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Human Metabolome Database Version 2.5

 

Showing metabocard for Sarcosine (HMDB00271)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-09-01 08:19:49
Accession Number HMDB00271
Secondary Accession Numbers Not Available
Common Name Sarcosine
Description Sarcosine is the N-methyl derivative of glycine. Sarcosine is metabolized to glycine by the enzyme sarcosine dehydrogenase, while glycine-N-methyl transferase generates sarcosine from glycine. Sarcosine is a natural amino acid found in muscles and other body tissues. In the laboratory it may be synthesized from chloroacetic acid and methylamine. Sarcosine is naturally found in the metabolism of choline to glycine. Sarcosine is sweet to the taste and dissolves in water. It is used in manufacturing biodegradable surfactants and toothpastes as well as in other applications. Sarcosine is ubiquitous in biological materials and is present in such foods as egg yolks, turkey, ham, vegetables, legumes, etc. Sarcosine is formed from dietary intake of choline and from the metabolism of methionine, and is rapidly degraded to glycine. Sarcosine has no known toxicity, as evidenced by the lack of phenotypic manifestations of sarcosinemia, an inborn error of sarcosine metabolism. Sarcosinemia can result from severe folate deficiency because of the folate requirement for the conversion of sarcosine to glycine (Wikipedia). Sarcosine has recently been identified as a biomarker for invasive prostate cancer. It was found to be greatly increased during prostate cancer progression to metastasis and could be detected in urine. Sarcosine levels were also increased in invasive prostate cancer cell lines relative to benign prostate epithelial cells.(PMID: 19212411)
Synonyms
  1. (Methylamino)acetate
  2. (Methylamino)acetic acid
  3. (Methylamino)ethanoate
  4. (Methylamino)ethanoic acid
  5. Methylglycine
  6. N-Methylaminoacetate
  7. N-Methylaminoacetic acid
  8. N-Methylglycine
  9. N-methyl-Glycine
  10. Sarcosin
  11. Sarcosinate
  12. Sarcosine
  13. Sarcosinic acid
  14. (methylamino)-Acetate
  15. (methylamino)-Acetic acid
Chemical IUPAC Name 2-methylaminoacetic acid
Chemical Formula C3H7NO2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Quaternary Amines
  • Amino Acids
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • secondary amine
  • secondary aliphatic amine (dialkylamine)
  • carboxylic acid
  • alpha-aminoacid
Biofunction
  • Component of Glycine, serine and threonine metabolism
Application
Source
  • Endogenous
Average Molecular Weight 89.093
Monoisotopic Molecular Weight 89.047676
Isomeric SMILES CNCC(O)=O
Canonical SMILES CNCC(O)=O
KEGG Compound ID C00213 Link Image
BioCyc ID SARCOSINE Link Image
BiGG ID 34275 Link Image
Wikipedia Link Sarcosine Link Image
NuGOwiki Link HMDB00271 Link Image
Metagene Link HMDB00271 Link Image
METLIN ID 51 Link Image
PubChem Compound 1088 Link Image
PubChem Substance 7994277 Link Image
ChEBI ID 15611 Link Image
CAS Registry Number 107-97-1
InChI Identifier InChI=1/C3H7NO2/c1-4-2-3(5)6/h4H,2H2,1H3,(H,5,6)
Synthesis Reference Cipens, G.; Slavinska, V.; Sile, D.; Kreile, D.; Strautina, A.; Krikis, A.; Gutmanis, A. Synthesis of sarcosine and its use. Latvijas PSR Zinatnu Akademijas Vestis, Kimijas Serija (1986), (5), 515-24.
Melting Point (Experimental) 208 oC
Experimental Water Solubility 300.0 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 308.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity -2.78 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity -3.06 [Predicted by ALOGPS]; -3 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • Extracellular
  • mitochondria
  • peroxisome
Biofluid Location
  • Blood
  • Saliva
  • Urine
Tissue Location
Tissue References
Muscle
Skeletal Muscle
Concentrations (Normal)
Biofluid Saliva
Value >10 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. [PubMed Link Image]
Biofluid Urine
Value 1.35 +/- 1.21 umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed Link Image]
Biofluid Urine
Value < 0.329 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Doctor's Data
Biofluid Urine
Value 0.47 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guo K, Li L: Differential (12)C-/(13)C-Isotope Dansylation Labeling and Fast Liquid Chromatography/Mass Spectrometry for Absolute and Relative Quantification of the Metabolome. Anal Chem. 2009 Mar 23. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 300.0 (80.0-603.0) uM
Age Children:1-13 yrs old
Sex Both
Condition Sarcosinemia
Comments Not Available
References
  • Levy HL, Coulombe JT, Benjamin R: Massachusetts Metabolic Disorders Screening Program: III. Sarcosinemia. Pediatrics. 1984 Oct;74(4):509-13. [PubMed Link Image]
Biofluid Blood
Value 312.5 (0.00-625.00) uM
Age Adult:>18 yrs old
Sex Both
Condition Sarcosinemia
Comments Not Available
References
Biofluid Blood
Value 405.00 (50.00-760.00) uM
Age Adult:>18 yrs old
Sex Both
Condition Sarcosinemia
Comments Not Available
References
Biofluid Urine
Value 1.8 (0.00-3.6) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Sarcosinemia
Comments Not Available
References
Biofluid Urine
Value 2660.00 (240.00-5080.00) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Sarcosinemia
Comments Not Available
References
Associated Disorders
Condition References
Sarcosinemia
  • 6207480
  • http://www.metagene.de/program/d.prg?mp=SARCOSINEMIA
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Glycine and Serine Metabolism SMP00004 Link Image map00260 Link Image
General References
  1. Boulat O, Gradwohl M, Matos V, Guignard JP, Bachmann C: Organic acids in the second morning urine in a healthy Swiss paediatric population. Clin Chem Lab Med. 2003 Dec;41(12):1642-58. [PubMed Link Image]
  2. Akare S, Martinez JD: Bile acid induces hydrophobicity-dependent membrane alterations. Biochim Biophys Acta. 2005 Jun 15;1735(1):59-67. [PubMed Link Image]
  3. Lim DS, Roberts R, Marian AJ: Expression profiling of cardiac genes in human hypertrophic cardiomyopathy: insight into the pathogenesis of phenotypes. J Am Coll Cardiol. 2001 Oct;38(4):1175-80. [PubMed Link Image]
  4. Bales JR, Sadler PJ, Nicholson JK, Timbrell JA: Urinary excretion of acetaminophen and its metabolites as studied by proton NMR spectroscopy. Clin Chem. 1984 Oct;30(10):1631-6. [PubMed Link Image]
  5. Heil M, Podebrad F, Prado E, Beck T, Mosand A, Sewell AC, Bohles H, Lehnert W: Enantioselective analysis of ketone bodies in patients with beta-ketothiolase deficiency, medium-chain acyl coenzyme A dehydrogenase deficiency and ketonemic vomiting. J Chromatogr B Biomed Sci Appl. 2000 Mar 10;739(2):313-24. [PubMed Link Image]
  6. Kang ES, Seyer J, Todd TA, Herrera C: Variability in the phenotypic expression of abnormal sarcosine metabolism in a family. Hum Genet. 1983;64(1):80-5. [PubMed Link Image]
  7. Vallera DA, Todhunter DA, Kuroki DW, Shu Y, Sicheneder A, Chen H: A bispecific recombinant immunotoxin, DT2219, targeting human CD19 and CD22 receptors in a mouse xenograft model of B-cell leukemia/lymphoma. Clin Cancer Res. 2005 May 15;11(10):3879-88. [PubMed Link Image]
  8. Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. [PubMed Link Image]
  9. Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed Link Image]
  10. Hitomi J, Yamaguchi K, Kikuchi Y, Kimura T, Maruyama K, Nagasaki K: A novel calcium-binding protein in amniotic fluid, CAAF1: its molecular cloning and tissue distribution. J Cell Sci. 1996 Apr;109 ( Pt 4):805-15. [PubMed Link Image]
  11. Wikipedia Link Image
Metabolic Enzymes
  1. Peroxisomal sarcosine oxidase
  2. Dimethylglycine dehydrogenase, mitochondrial
  3. Glycine N-methyltransferase
  4. Sarcosine dehydrogenase, mitochondrial
  5. cDNA FLJ14592 fis, clone NT2RM4002063, highly similar to Peroxisomal sarcosine oxidase (EC 1.5.3.1)
  6. Sarcosine dehydrogenase
  7. Proton-coupled amino acid transporter 2
Enzyme 1 [top]
Enzyme 1 ID 5354
Enzyme 1 Name Peroxisomal sarcosine oxidase
Enzyme 1 Synonyms
  1. PSO
  2. L-pipecolate oxidase
  3. L-pipecolic acid oxidase
Enzyme 1 Gene Name PIPOX
Enzyme 1 Protein Sequence >Peroxisomal sarcosine oxidase
MAAQKDLWDAIVIGAGIQGCFTAYHLAKHRKRILLLEQFFLPHSRGSSHGQSRIIRKAYL
EDFYTRMMHECYQIWAQLEHEAGTQLHRQTGLLLLGMKENQELKTIQANLSRQRVEHQCL
SSEELKQRFPNIRLPRGEVGLLDNSGGVIYAYKALRALQDAIRQLGGIVRDGEKVVEINP
GLLVTVKTTSRSYQAKSLVITAGPWTNQLLRPLGIEMPLQTLRINVCYWREMVPGSYGVS
QAFPCFLWLGLCPHHIYGLPTGEYPGLMKVSYHHGNHADPEERDCPTARTDIGDVQILSS
FVRDHLPDLKPEPAVIESCMYTNTPDEQFILDRHPKYDNIVIGAGFSGHGFKLAPVVGKI
LYELSMKLTPSYDLAPFRISRFPSLGKAHL
Enzyme 1 Number of Residues 390
Enzyme 1 Molecular Weight 44065.5
Enzyme 1 Theoretical pI 8.54
Enzyme 1 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • oxidoreductase activity, acting on the CH-NH group of donors, oxygen as acceptor
  • sarcosine oxidase activity
Process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • folic acid and derivative metabolic process
  • metabolic process
  • oxidation reduction
  • tetrahydrofolate metabolic process
Component
Enzyme 1 General Function Involved in oxidoreductase activity
Enzyme 1 Specific Function Metabolizes sarcosine, L-pipecolic acid and L-proline
Enzyme 1 Pathways
Enzyme 1 Reactions
  • L-pipecolate + O2 = 2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2 [RN:R02204]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 7157903 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q9P0Z9 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name SOX_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1173 bp
ATGGCGGCTCAGAAAGATCTCTGGGACGCCATTGTGATTGGGGCGGGGATCCAGGGCTGC
TTCACTGCATACCACCTCGCCAAACACAGGAAGAGGATCCTCCTGCTGGAGCAGTTCTTT
CTACCACACTCCCGAGGAAGCTCCCATGGACAAAGCCGGATAATCCGAAAGGCGTACCTG
GAAGACTTTTACACCCGGATGATGCATGAGTGCTATCAGATATGGGCCCAGCTGGAGCAC
GAGGCTGGAACCCAATTGCACAGGCAGACTGGATTACTGCTGCTGGGAATGAAAGAGAAT
CAAGAATTAAAGACAATCCAGGCCAATCTGTCGAGGCAGAGGGTAGAACACCAGTGTCTT
TCATCTGAGGAACTGAAGCAACGTTTCCCAAATATTCGGTTGCCCAGGGGAGAAGTGGGG
CTCTTGGACAATTCCGGAGGAGTTATCTATGCATATAAGGCCCTCAGAGCCCTGCAGGAT
GCAATTCGACAGCTAGGAGGCATAGTGCGTGACGGAGAGAAGGTGGTGGAGATAAACCCA
GGGCTACTGGTCACGGTGAAAACCACCTCCAGGAGCTACCAAGCTAAGAGCTTGGTCATC
ACAGCAGGTCCTTGGACCAACCAGCTCCTCCGTCCCCTGGGCATTGAGATGCCTCTCCAG
ACCCTGCGGATCAACGTGTGTTACTGGCGAGAGATGGTTCCTGGGAGCTATGGTGTGTCC
CAGGCCTTTCCGTGCTTCCTGTGGCTGGGCTTGTGTCCCCACCACATCTACGGACTGCCC
ACAGGAGAGTACCCAGGGCTGATGAAGGTCAGCTATCACCACGGCAACCACGCAGACCCT
GAGGAGCGGGACTGCCCCACAGCACGCACAGACATCGGAGACGTCCAGATCCTGAGCAGC
TTTGTCAGAGATCACTTACCTGATCTGAAGCCCGAGCCTGCTGTCATTGAGAGCTGCATG
TACACGAATACCCCTGATGAGCAGTTCATTCTCGATCGCCACCCAAAGTATGACAACATT
GTCATTGGTGCTGGATTCTCTGGGCACGGGTTCAAGCTGGCCCCTGTGGTGGGGAAGATC
CTGTATGAATTAAGCATGAAATTAACACCATCTTATGACTTGGCACCTTTTCGAATCAGC
CGTTTCCCAAGCCTGGCCAAAGCCCACCTGTGA
Enzyme 1 GenBank Gene ID AF134593 Link Image
Enzyme 1 GeneCard ID PIPOX Link Image
Enzyme 1 GenAtlas ID PIPOX Link Image
Enzyme 1 HGNC ID HGNC:17804 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 17q11.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. IJlst L, de Kromme I, Oostheim W, Wanders RJ: Molecular cloning and expression of human L-pipecolate oxidase. Biochem Biophys Res Commun. 2000 Apr 21;270(3):1101-5. [PubMed Link Image]
  2. Dodt G, Kim DG, Reimann SA, Reuber BE, McCabe K, Gould SJ, Mihalik SJ: L-Pipecolic acid oxidase, a human enzyme essential for the degradation of L-pipecolic acid, is most similar to the monomeric sarcosine oxidases. Biochem J. 2000 Feb 1;345 Pt 3:487-94. [PubMed Link Image]
  3. Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5435
Enzyme 2 Name Dimethylglycine dehydrogenase, mitochondrial
Enzyme 2 Synonyms
  1. ME2GLYDH
Enzyme 2 Gene Name DMGDH
Enzyme 2 Protein Sequence >Dimethylglycine dehydrogenase, mitochondrial
MLRPGAQLLRGLLLRSCPLQGSPGRPRSVCGREGEEKPPLSAETQWKDRAETVIIGGGCV
GVSLAYHLAKAGMKDVVLLEKSELTAGSTWHAAGLTTYFHPGINLKKIHYDSIKLYEKLE
EETGQVVGFHQPGSIRLATTPVRVDEFKYQMTRTGWHATEQYLIEPEKIQEMFPLLNMNK
VLAGLYNPGDGHIDPYSLTMALAAGARKCGALLKYPAPVTSLKARSDGTWDVETPQGSMR
ANRIVNAAGFWAREVGKMIGLEHPLIPVQHQYVVTSTISEVKALKRELPVLRDLEGSYYL
RQERDGLLFGPYESQEKMKVQDSWVTNGVPPGFGKELFESDLDRIMEHIKAAMEMVPVLK
KADIINVVNGPITYSPDILPMVGPHQGVRNYWVAIGFGYGIIHAGGVGKYLSDWILHGEP
PFDLIELDPNRYGKWTTTQYTEAKARESYGFNNIVGYPKEERFAGRPTQRVSGLYQRLES
KCSMGFHAGWEQPHWFYKPGQDTQYRPSFRRTNWFEPVGSEYKQVMQRVAVTDLSPFGKF
NIKGQDSIRLLDHLFANVIPKVGFTNISHMLTPKGRVYAELTVSHQSPGEFLLITGSGSE
LHDLRWIEEEAVKGGYDVEIKNITDELGVLGVAGPQARKVLQKLTSEDLSDDVFKFLQTK
SLKVSNIPVTAIRISYTGELGWELYHRREDSVALYDAIMNAGQEEGIDNFGTYAMNALRL
EKAFRAWGLEMNCDTNPLEAGLEYFVKLNKPADFIGKQALKQIKAKGLKRRLVCLTLATD
DVDPEGNESIWYNGKVVGNTTSGSYSYSIQKSLAFAYVPVQLSEVGQQVEVELLGKNYPA
VIIQEPLVLTEPTRNRLQKKGGKDKT
Enzyme 2 Number of Residues 866
Enzyme 2 Molecular Weight 96810.1
Enzyme 2 Theoretical pI 7.69
Enzyme 2 GO Classification
Function
  • aminomethyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • oxidoreductase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • glycine catabolic process
  • glycine metabolic process
  • metabolic process
  • serine family amino acid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 2 General Function Involved in oxidoreductase activity
Enzyme 2 Specific Function N,N-dimethylglycine + acceptor + H(2)O = sarcosine + formaldehyde + reduced acceptor
Enzyme 2 Pathways
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 2 Reactions
  • N,N-dimethylglycine + acceptor + H2O = sarcosine + formaldehyde + reduced acceptor [RN:R01565]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 24797151 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9UI17 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name M2GD_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >2601 bp
ATGCTCCGTCCCGGCGCGCAGCTGCTGCGGGGCCTCCTGCTGCGGAGCTGCCCGCTGCAG
GGCTCCCCCGGGCGCCCGCGCTCTGTCTGCGGCCGGGAAGGAGAGGAAAAACCACCCTTA
TCTGCAGAAACACAATGGAAAGACAGAGCAGAAACAGTGATAATTGGAGGTGGCTGTGTT
GGTGTGAGTCTGGCTTATCACCTGGCCAAAGCAGGGATGAAAGATGTGGTCCTGCTGGAG
AAATCAGAGCTCACGGCTGGATCTACCTGGCACGCAGCAGGTTTAACAACTTACTTTCAT
CCTGGAATAAACTTGAAGAAAATACATTATGATAGCATCAAACTTTATGAGAAACTGGAA
GAAGAAACTGGTCAGGTGGTGGGATTCCATCAGCCAGGTAGTATCAGACTTGCTACCACC
CCTGTAAGGGTAGATGAATTTAAATATCAAATGACTCGGACTGGCTGGCATGCAACAGAA
CAGTATCTCATTGAACCTGAAAAAATTCAAGAGATGTTCCCTTTACTCAACATGAATAAG
GTTTTAGCTGGATTGTATAATCCTGGAGATGGTCACATTGATCCTTATTCTCTAACTATG
GCACTGGCTGCTGGGGCTAGGAAATGTGGTGCCCTTTTAAAATATCCTGCACCAGTAACT
TCTCTGAAAGCCAGGTCAGATGGAACATGGGACGTTGAAACACCACAGGGGTCTATGAGA
GCAAATAGAATTGTGAATGCTGCAGGATTTTGGGCTCGTGAAGTAGGTAAAATGATTGGA
CTAGAACATCCTCTCATTCCGGTTCAACATCAATATGTTGTTACATCGACTATATCTGAA
GTGAAAGCTTTGAAACGAGAACTGCCTGTGCTCCGTGACCTGGAAGGATCATATTATCTC
CGACAGGAAAGGGATGGGCTTTTGTTTGGTCCATATGAAAGTCAAGAGAAAATGAAAGTT
CAGGACTCCTGGGTCACCAATGGAGTTCCTCCAGGTTTTGGAAAGGAACTCTTTGAGTCT
GATCTAGATCGAATCATGGAACACATCAAAGCTGCCATGGAAATGGTTCCTGTCTTGAAA
AAGGCTGACATCATCAATGTTGTCAATGGTCCTATCACGTATTCTCCTGACATTCTGCCT
ATGGTGGGGCCCCATCAGGGGGTCAGAAACTACTGGGTGGCTATAGGCTTTGGATATGGC
ATAATCCACGCTGGTGGGGTAGGGAAATATCTCAGTGACTGGATCCTGCATGGAGAACCT
CCTTTTGATCTGATAGAATTGGATCCTAATCGCTATGGCAAATGGACAACAACCCAGTAC
ACTGAGGCCAAAGCAAGAGAATCATATGGATTCAACAATATTGTTGGTTATCCTAAAGAA
GAACGGTTTGCTGGGAGGCCGACTCAACGAGTCAGTGGGCTCTATCAAAGGCTGGAGTCT
AAGTGTTCCATGGGGTTCCATGCTGGCTGGGAGCAGCCGCACTGGTTCTACAAACCAGGC
CAGGACACTCAGTACAGGCCAAGTTTTCGCCGCACAAACTGGTTTGAGCCTGTGGGCTCG
GAGTATAAACAGGTTATGCAAAGAGTAGCGGTAACTGACCTATCACCATTTGGCAAGTTT
AACATCAAAGGCCAAGATTCCATTAGACTACTGGACCATCTCTTTGCAAATGTCATTCCA
AAGGTGGGTTTTACAAATATAAGTCACATGTTAACACCCAAGGGTCGAGTGTATGCTGAG
CTGACTGTTTCTCACCAATCTCCTGGGGAGTTTCTTTTAATTACTGGCTCTGGATCAGAA
CTTCATGATCTTAGATGGATTGAAGAAGAAGCAGTCAAAGGTGGATATGATGTTGAAATT
AAAAACATAACTGATGAGCTTGGAGTTCTTGGAGTTGCTGGGCCACAGGCAAGAAAGGTC
CTTCAGAAACTGACCTCTGAAGATCTTAGTGATGATGTTTTCAAGTTTCTTCAAACCAAG
TCCTTAAAGGTTTCCAACATTCCTGTCACTGCTATTAGGATATCTTATACTGGTGAGCTG
GGTTGGGAGCTGTATCACAGAAGAGAAGATTCTGTGGCGCTGTATGACGCTATCATGAAT
GCAGGCCAGGAGGAGGGAATCGACAATTTTGGAACCTATGCCATGAATGCCTTACGCCTG
GAGAAAGCCTTCAGAGCCTGGGGGTTAGAGATGAACTGTGATACAAATCCTTTGGAAGCT
GGACTGGAATATTTTGTGAAGTTAAATAAGCCAGCAGACTTCATAGGAAAGCAAGCACTG
AAACAGATTAAAGCCAAGGGGCTGAAACGAAGACTGGTCTGCCTCACCTTGGCAACGGAT
GATGTTGATCCAGAGGGAAATGAAAGCATCTGGTACAATGGCAAGGTGGTTGGCAACACG
ACATCTGGAAGCTATAGCTACAGCATCCAGAAGAGTCTGGCTTTCGCATATGTCCCTGTA
CAACTAAGTGAAGTGGGACAGCAAGTGGAAGTTGAACTATTAGGCAAAAATTACCCAGCA
GTCATCATACAAGAACCTTTGGTATTGACCGAACCAACCAGAAACCGGCTTCAGAAAAAA
GGTGGAAAGGACAAAACTTGA
Enzyme 2 GenBank Gene ID NM_013391.2 Link Image
Enzyme 2 GeneCard ID DMGDH Link Image
Enzyme 2 GenAtlas ID DMGDH Link Image
Enzyme 2 HGNC ID HGNC:24475 Link Image
Enzyme 2 Chromosome Location 5
Enzyme 2 Locus 5q14.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Binzak BA, Vockley JG, Jenkins RB, Vockley J: Structure and analysis of the human dimethylglycine dehydrogenase gene. Mol Genet Metab. 2000 Mar;69(3):181-7. [PubMed Link Image]
  2. Binzak BA, Wevers RA, Moolenaar SH, Lee YM, Hwu WL, Poggi-Bach J, Engelke UF, Hoard HM, Vockley JG, Vockley J: Cloning of dimethylglycine dehydrogenase and a new human inborn error of metabolism, dimethylglycine dehydrogenase deficiency. Am J Hum Genet. 2001 Apr;68(4):839-47. Epub 2001 Feb 28. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed Link Image]
  5. Moolenaar SH, Poggi-Bach J, Engelke UF, Corstiaensen JM, Heerschap A, de Jong JG, Binzak BA, Vockley J, Wevers RA: Defect in dimethylglycine dehydrogenase, a new inborn error of metabolism: NMR spectroscopy study. Clin Chem. 1999 Apr;45(4):459-64. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5640
Enzyme 3 Name Glycine N-methyltransferase
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name GNMT
Enzyme 3 Protein Sequence >Glycine N-methyltransferase
MVDSVYRTRSLGVAAEGLPDQYADGEAARVWQLYIGDTRSRTAEYKAWLLGLLRQHGCQR
VLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYALKERWNRRHEPAFDKWVIEEANWMT
LDKDVPQSAEGGFDAVICLGNSFAHLPDCKGDQSEHRLALKNIASMVRAGGLLVIDHRNY
DHILSTGCAPPGKNIYYKSDLTKDVTTSVLIVNNKAHMVTLDYTVQVPGAGQDGSPGLSK
FRLSYYPHCLASFTELLQAAFGGKCQHSVLGDFKPYKPGQTYIPCYFIHVLKRTD
Enzyme 3 Number of Residues 295
Enzyme 3 Molecular Weight 32742.0
Enzyme 3 Theoretical pI 7.03
Enzyme 3 GO Classification
Function
  • N-methyltransferase activity
  • amino acid binding
  • binding
  • carboxylic acid binding
  • catalytic activity
  • folic acid binding
  • glycine N-methyltransferase activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • methionine metabolic process
  • sulfur amino acid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 3 General Function Involved in folic acid binding
Enzyme 3 Specific Function Catalyzes the methylation of glycine by using S- adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with the concomitant production of S-adenosylhomocysteine (AdoHcy). Possible crucial role in the regulation of tissue concentration of AdoMet and of metabolism of methionine
Enzyme 3 Pathways
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 3 Reactions
  • S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine [RN:R00367]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 8671584 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q14749 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name GNMT_HUMAN Link Image
Enzyme 3 PDB ID 1R74 Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >888 bp
ATGGTGGACAGCGTGTACCGGACCCGCTCCCTGGGGGTGGCGGCCGAAGGGCTCCCGGAC
CAGTACGCGGACGGGGAGGCGGCGCGCGTGTGGCAGCTGTATATCGGAGACACCCGCAGC
CGCACCGCCGAGTACAAGGCATGGCTGCTTGGGCTGCTGCGCCAGCACGGCTGCCAGCGG
GTGCTCGACGTAGCCTGTGGCACTGGGGTGGACTCCATTATGCTGGTGGAAGAGGGCTTC
AGTGTGACGAGTGTGGATGCCAGTGACAAGATGCTGAAGTATGCACTTAAGGAGCGCTGG
AACCGGCGGCACGAGCCCGCCTTCGACAAGTGGGTCATCGAAGAAGCCAACTGGATGACT
CTGGACAAAGATGTGCCCCAGTCAGCAGAGGGTGGCTTTGATGCTGTCATCTGCCTTGGA
AACAGTTTCGCTCACTTGCCAGACTGCAAAGGGGACCAGAGTGAGCACCGGCTGGCGCTG
AAAAACATTGCGAGCATGGTGCGGGCAGGGGGCCTACTGGTCATTGATCATCGCAACTAC
GACCACATCCTCAGTACAGGCTGTGCACCCCCAGGGAAGAACATCTACTATAAGAGTGAC
TTGACCAAGGACGTCACAACATCAGTGCTGATAGTGAACAACAAGGCCCACATGGTGACC
CTGGACTATACGGTGCAGGTGCCGGGGGCTGGCCAGGATGGCTCTCCTGGCTTGAGTAAG
TTCCGGCTCTCCTACTACCCACACTGTCTGGCATCCTTCACGGAGCTGCTCCAAGCAGCC
TTCGGAGGTAAGTGCCAGCACAGCGTCCTGGGCGACTTCAAGCCTTACAAGCCAGGCCAA
ACCTACATTCCCTGCTACTTCATCCACGTGCTCAAGAGGACAGACTGA
Enzyme 3 GenBank Gene ID AF101477 Link Image
Enzyme 3 GeneCard ID GNMT Link Image
Enzyme 3 GenAtlas ID GNMT Link Image
Enzyme 3 HGNC ID HGNC:4415 Link Image
Enzyme 3 Chromosome Location 6
Enzyme 3 Locus 6p12
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Chen YM, Shiu JY, Tzeng SJ, Shih LS, Chen YJ, Lui WY, Chen PH: Characterization of glycine-N-methyltransferase-gene expression in human hepatocellular carcinoma. Int J Cancer. 1998 Mar 2;75(5):787-93. [PubMed Link Image]
  2. Chen YM, Chen LY, Wong FH, Lee CM, Chang TJ, Yang-Feng TL: Genomic structure, expression, and chromosomal localization of the human glycine N-methyltransferase gene. Genomics. 2000 May 15;66(1):43-7. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Ogawa H, Gomi T, Fujioka M: Mammalian glycine N-methyltransferases. Comparative kinetic and structural properties of the enzymes from human, rat, rabbit and pig livers. Comp Biochem Physiol B. 1993 Nov;106(3):601-11. [PubMed Link Image]
  6. Pakhomova S, Luka Z, Grohmann S, Wagner C, Newcomer ME: Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes. Proteins. 2004 Nov 1;57(2):331-7. [PubMed Link Image]
  7. Luka Z, Pakhomova S, Luka Y, Newcomer ME, Wagner C: Destabilization of human glycine N-methyltransferase by H176N mutation. Protein Sci. 2007 Sep;16(9):1957-64. Epub 2007 Jul 27. [PubMed Link Image]
  8. Luka Z, Cerone R, Phillips JA 3rd, Mudd HS, Wagner C: Mutations in human glycine N-methyltransferase give insights into its role in methionine metabolism. Hum Genet. 2002 Jan;110(1):68-74. Epub 2001 Dec 7. [PubMed Link Image]
  9. Luka Z, Wagner C: Effect of naturally occurring mutations in human glycine N-methyltransferase on activity and conformation. Biochem Biophys Res Commun. 2003 Dec 26;312(4):1067-72. [PubMed Link Image]
  10. Augoustides-Savvopoulou P, Luka Z, Karyda S, Stabler SP, Allen RH, Patsiaoura K, Wagner C, Mudd SH: Glycine N -methyltransferase deficiency: a new patient with a novel mutation. J Inherit Metab Dis. 2003;26(8):745-59. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6073
Enzyme 4 Name Sarcosine dehydrogenase, mitochondrial
Enzyme 4 Synonyms
  1. SarDH
  2. BPR-2
Enzyme 4 Gene Name SARDH
Enzyme 4 Protein Sequence >Sarcosine dehydrogenase, mitochondrial
MASLSRALRVAAAHPRQSPTRGMGPCNLSSAAGPTAEKSVPYQRTLKEGQGTSVVAQGPS
RPLPSTANVVVIGGGSLGCQTLYHLAKLGMSGAVLLERERLTSGTTWHTAGLLWQLRPSD
VEVELLAHTRRVVSRELEEETGLHTGWIQNGGLFIASNRQRLDEYKRLMSLGKAYGVESH
VLSPAETKTLYPLMNVDDLYGTLYVPHDGTMDPAGTCTTLARAASARGAQVIENCPVTGI
RVWTDDFGVRRVAGVETQHGSIQTPCVVNCAGVWASAVGRMAGVKVPLVAMHHAYVVTER
IEGIQNMPNVRDHDASVYLRLQGDALSVGGYEANPIFWEEVSDKFAFGLFDLDWEVFTQH
IEGAINRVPVLEKTGIKSTVCGPESFTPDHKPLMGEAPELRGFFLGCGFNSAGMMLGGGC
GQELAHWIIHGRPEKDMHGYDIRRFHHSLTDHPRWIRERSHESYAKNYSVVFPHDEPLAG
RNMRRDPLHEELLGQGCVFQERHGWERPGWFHPRGPAPVLEYDYYGAYGSRAHEDYAYRR
LLADEYTFAFPPHHDTIKKECLACRGAAAVFDMSYFGKFYLVGLDARKAADWLFSADVSR
PPGSTVYTCMLNHRGGTESDLTVSRLAPSHQASPLAPAFEGDGYYLAMGGAVAQHNWSHI
TTVLQDQKSQCQLIDSSEDLGMISIQGPASRAILQEVLDADLSNEAFPFSTHKLLRAAGH
LVRAMRLSFVGELGWELHIPKASCVPVYRAVMAAGAKHGLINAGYRAIDSLSIEKGYRHW
HADLRPDDSPLEAGLAFTCKLKSPVPFLGREALEQQRAAGLRRRLVCFTMEDKVPMFGLE
AIWRNGQVVGHVRRADFGFAIDKTIAYGYIHDPSGGPVSLDFVKSGDYALERMGVTYGAQ
AHLKSPFDPNNKRVKGIY
Enzyme 4 Number of Residues 918
Enzyme 4 Molecular Weight 101036.0
Enzyme 4 Theoretical pI 7.26
Enzyme 4 GO Classification
Function
  • aminomethyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • oxidoreductase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • glycine catabolic process
  • glycine metabolic process
  • metabolic process
  • serine family amino acid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 4 General Function Involved in oxidoreductase activity
Enzyme 4 Specific Function Sarcosine + acceptor + H(2)O = glycine + formaldehyde + reduced acceptor
Enzyme 4 Pathways
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 4 Reactions
  • sarcosine + acceptor + H2O = glycine + formaldehyde + reduced acceptor [RN:R00611]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 5902974 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9UL12 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name SARDH_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >2757 bp
ATGGCCTCACTGAGCCGAGCCCTACGTGTGGCTGCTGCCCACCCTCGCCAGAGCCCTACC
CGGGGCATGGGGCCATGCAACCTGTCCAGCGCAGCTGGCCCCACAGCCGAGAAGAGTGTG
CCATATCAGCGGACCCTGAAGGAGGGACAGGGCACCTCGGTGGTGGCCCAAGGCCCAAGC
CGGCCCCTGCCCAGCACGGCCAACGTGGTGGTCATTGGTGGAGGCAGCTTGGGCTGCCAG
ACCCTGTACCACCTGGCCAAGCTGGGCATGAGTGGGGCGGTGCTGCTGGAGCGGGAGCGG
CTGACCTCCGGGACCACCTGGCACACGGCAGGCCTGCTGTGGCAGCTGCGGCCCAGTGAC
GTGGAGGTGGAGCTTCTGGCCCACACTCGGCGGGTGGTGAGCCGGGAGCTGGAGGAGGAG
ACGGGACTACACACGGGCTGGATCCAGAATGGGGGCCTCTTCATCGCGTCCAACCGGCAG
CGCCTGGACGAGTACAAGAGGCTCATGTCGCTGGGCAAGGCGTATGGTGTGGAATCCCAT
GTGCTGAGCCCGGCAGAGACCAAGACTCTGTACCCGCTGATGAATGTGGACGACCTCTAC
GGGACCCTGTATGTGCCGCACGACGGTACCATGGACCCCGCTGGCACCTGTACCACCCTC
GCCAGGGCAGCTTCTGCCCGAGGAGCACAGGTCATTGAGAACTGCCCAGTGACCGGCATT
CGTGTGTGGACGGATGATTTTGGGGTGCGGCGGGTCGCGGGTGTGGAGACTCAGCATGGT
TCCATCCAGACACCCTGCGTGGTCAACTGTGCAGGAGTGTGGGCAAGTGCTGTGGGCCGG
ATGGCTGGAGTCAAGGTCCCGCTGGTGGCCATGCACCATGCCTATGTCGTCACCGAGCGC
ATCGAGGGGATTCAGAACATGCCCAATGTCCGTGATCATGATGCCTCTGTCTACCTCCGC
CTCCAAGGGGATGCCTTGTCTGTGGGTGGCTATGAGGCCAACCCCATCTTTTGGGAGGAG
GTGTCAGACAAGTTTGCCTTCGGCCTCTTTGACCTGGACTGGGAGGTGTTCACCCAGCAC
ATTGAAGGCGCCATCAACAGGGTCCCCGTGCTGGAGAAGACAGGAATCAAGTCCACGGTC
TGCGGCCCTGAATCCTTCACGCCCGACCACAAGCCCCTGATGGGGGAGGCACCTGAGCTC
CGAGGGTTCTTCCTGGGCTGTGGCTTCAACAGCGCAGGAATGATGCTGGGTGGTGGCTGT
GGGCAGGAGCTGGCCCACTGGATCATCCATGGGCGCCCGGAGAAGGACATGCATGGCTAT
GACATCAGGCGCTTCCATCACTCGCTCACGGACCACCCCCGCTGGATCCGAGAGCGAAGC
CATGAGTCCTACGCCAAGAACTACTCCGTCGTCTTCCCCCACGATGAGCCGCTGGCCGGG
CGCAACATGAGGAGAGACCCGCTGCATGAGGAACTCCTTGGACAAGGCTGCGTGTTCCAG
GAGCGGCATGGCTGGGAGCGACCGGGATGGTTTCATCCCCGAGGCCCAGCTCCGGTCCTC
GAGTACGACTACTACGGGGCTTACGGGAGCCGCGCGCACGAGGACTACGCCTACCGCAGG
CTGCTGGCAGACGAGTACACCTTCGCCTTCCCGCCCCACCACGACACGATCAAGAAGGAG
TGCCTGGCCTGCAGAGGGGCCGCCGCTGTGTTTGACATGTCCTACTTCGGGAAGTTCTAC
CTGGTGGGGCTGGATGCAAGGAAGGCTGCCGACTGGCTCTTCTCCGCAGATGTCAGCCGA
CCCCCAGGCTCCACCGTGTACACGTGCATGCTCAACCACCGTGGGGGCACCGAGAGTGAC
CTGACTGTCAGCCGCCTGGCACCCAGCCACCAGGCCTCCCCGCTGGCCCCCGCCTTTGAA
GGGGACGGTTACTACCTGGCCATGGGCGGGGCCGTGGCCCAGCACAACTGGTCCCACATC
ACCACCGTGCTGCAGGACCAGAAGTCCCAGTGCCAGCTCATCGACAGCTCCGAGGACCTG
GGTATGATCAGTATCCAGGGCCCAGCCAGCCGAGCCATTTTGCAGGAGGTGCTGGACGCA
GACCTGAGCAACGAGGCCTTCCCGTTCTCCACCCACAAGCTACTGAGAGCCGCAGGGCAC
CTGGTCCGAGCCATGCGGCTGTCCTTTGTGGGGGAGCTGGGCTGGGAGCTGCACATTCCA
AAGGCGTCCTGCGTGCCTGTGTACCGGGCTGTGATGGCCGCGGGTGCCAAGCACGGCCTC
ATCAACGCAGGGTACCGCGCCATCGACTCCCTGAGCATTGAGAAAGGCTACCGGCACTGG
CACGCGGACCTGCGGCCAGACGACAGCCCCCTGGAGGCAGGCCTGGCCTTCACCTGCAAG
CTCAAGTCGCCGGTGCCCTTCCTGGGGAGGGAGGCCCTGGAGCAGCAGCGGGCCGCAGGC
CTCCGCCGGCGCCTGGTGTGCTTCACCATGGAGGACAAAGTACCCATGTTTGGCCTGGAG
GCCATCTGGAGGAACGGCCAAGTGGTGGGCCATGTCCGGAGGGCTGACTTTGGGTTCGCC
ATCGACAAGACCATCGCCTACGGTTACATCCATGACCCCAGCGGTGGGCCGGTCTCGCTG
GACTTTGTGAAGAGCGGGGACTATGCCCTGGAGAGAATGGGGGTGACCTATGGTGCCCAG
GCTCACCTGAAGTCGCCCTTCGACCCCAACAACAAGAGGGTGAAGGGAATCTACTGA
Enzyme 4 GenBank Gene ID AF095735 Link Image
Enzyme 4 GeneCard ID SARDH Link Image
Enzyme 4 GenAtlas ID SARDH Link Image
Enzyme 4 HGNC ID HGNC:10536 Link Image
Enzyme 4 Chromosome Location 9
Enzyme 4 Locus 9q33-q34
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Eschenbrenner M, Jorns MS: Cloning and mapping of the cDNA for human sarcosine dehydrogenase, a flavoenzyme defective in patients with sarcosinemia. Genomics. 1999 Aug 1;59(3):300-8. [PubMed Link Image]
  2. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Gilbert JR, Kumar A, Newey S, Rao N, Ioannou P, Qiu H, Lin D, Xu P, Pettenati MJ, Pericak-Vance MA: Physical and cDNA mapping in the DBH region of human chromosome 9q34. Hum Hered. 2000 May-Jun;50(3):151-7. [PubMed Link Image]
  5. Tang LY, Deng N, Wang LS, Dai J, Wang ZL, Jiang XS, Li SJ, Li L, Sheng QH, Wu DQ, Li L, Zeng R: Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction. Mol Cell Proteomics. 2007 Nov;6(11):1952-67. Epub 2007 Aug 12. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 16475
Enzyme 5 Name cDNA FLJ14592 fis, clone NT2RM4002063, highly similar to Peroxisomal sarcosine oxidase (EC 1.5.3.1)
Enzyme 5 Synonyms
  1. SubName: Pipecolic acid oxidase, isoform CRA_b
Enzyme 5 Gene Name PIPOX
Enzyme 5 Protein Sequence >cDNA FLJ14592 fis, clone NT2RM4002063, highly similar to Peroxisomal sarcosine oxidase (EC 1.5.3.1)
MAAQKDLWDAIVIGAGIQGCFTAYHLAKHRKRILLLEQFFLPHSRGSSHGQSRIIRKAYL
EDFYTRMMHECYQIWAQLEHEAGTQLHRQTGLLLLGMKENQELKTIQANLSRQRVEHQCL
SSEELKQRFPNIRLPRGEVGLLDNSGGVIYAYKALRALQDAIRQLGGIVRDGEKVVEINP
GLLVTVKTTSRSYQAKSLVITAGPWTNQLLRPLGIEMPLQTLRINVCYWREMVPGSYGVS
QAFPCFLWLGLCPHHIYGLPTGEYPGLMKVSYHHGNHADPEERDCPTARTDIGDVQILSS
FVRDHLPDLKPEPAVIESCMYTNTPDEQFILDRHPKYDNIVIGAGFSGHGFKLAPVVGKI
LYELSMKLTPSYDLAPFRISRFPSLGKAHL
Enzyme 5 Number of Residues 390
Enzyme 5 Molecular Weight 44067
Enzyme 5 Theoretical pI 8.54
Enzyme 5 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • oxidoreductase activity, acting on the CH-NH group of donors, oxygen as acceptor
  • sarcosine oxidase activity
Process
  • aromatic compound metabolism
  • cellular metabolism
  • electron transport
  • folic acid and derivative metabolism
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
  • tetrahydrofolate metabolism
Component
Enzyme 5 General Function Amino acid transport and metabolism
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions
  • sarcosine + H2O + O2 = glycine + formaldehyde + H2O2 [RN:R00610] ALL_REAC R00610
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID B3KNH0 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name B3KNH0_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID AK027498 Link Image
Enzyme 5 GeneCard ID B3KNH0 Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location 17
Enzyme 5 Locus 17q11.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 16490
Enzyme 6 Name Sarcosine dehydrogenase
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name SARDH
Enzyme 6 Protein Sequence >Sarcosine dehydrogenase
MASLSRALRVAAAHPRQSPTRGMGPCNLSSAAGPTAEKSVPYQRTLKEGQGTSVVAQGPS
RPLPSTANVVVIGGGSLGCQTLYHLAKLGMSGAVLLERERLTSGTTWHTAGLLWQLRPSD
VEVELLAHTRRVVSRELEEETGLHTGWIQNGGLFIASNRQRLDEYKRLMSLGKAYGVESH
VLSPAETKTLYPLMNVDDLYGTLYVPHDGTMDPAGTCTTLARAASARGAQVIENCPVTGI
RVWTDDFGVRRVAGVETQHGSIQTPCVVNCAGVWASAVGRMAGVKVPLVAMHHAYVVTER
IEGIQNMPNVRDHDASVYLRLQGDALSVGGYEANPIFWEEVSDKFAFGLFDLDWEVFTQH
IEGAINRVPVLEKTGIKSTVCGPESFTPDHKPLMGEAPELRGFFLGCGFNSAGMMLGGGC
GQELAHWIIHGRPEKDMHGYDIRRFHHSLTDHPRWIRERSHESYAKNYSVVFPHDEPLAG
RNMRRDPLHEELLGQGCVFQERHGWERPGWFHPRGPAPVLEYDYYGAYGSRAHEDYAYRR
LLADEYTFAFPPHHDTIKKECLACRGAAAVFDMSYFGKFYLVGLDARKAADWLFSADVSR
PPGSTVYTCMLNHRGGTESDLTVSRLAPSHQASPLAPAFEGDGYYLAMGGAVAQHNWSHI
TTVLQDQKSQCQLIDSSEDLGMISIQGPASRAILQEVLDADLSNEAFPFSTHKLLRAAGH
LVRAMRLSFVGELGWELHIPKASCVPVYRAVMAAGAKHGLINAGYRAIDSLSIEKGYRHW
HADLRPDDSPLEAGLAFTCKLKSPVPFLGREALEQQRAAGLRRRLVCFTMEDKVPMFGLE
AIWRNGQVVGHVRRADFGFAIDKTIAYGYIHDPSGGPVSLDFVKSGDYALERMGVTYGAQ
AHLKSPFDPNNKRVKGIY
Enzyme 6 Number of Residues 918
Enzyme 6 Molecular Weight 101038
Enzyme 6 Theoretical pI 7.26
Enzyme 6 GO Classification
Function
  • aminomethyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • oxidoreductase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • glycine catabolism
  • glycine metabolism
  • metabolism
  • physiological process
  • serine family amino acid metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 6 General Function Amino acid transport and metabolism
Enzyme 6 Specific Function Not Available
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein Not Available
Enzyme 6 UniProtKB/Swiss-Prot ID B2RMR5 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name B2RMR5_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence Not Available
Enzyme 6 GenBank Gene ID BC136363 Link Image
Enzyme 6 GeneCard ID B2RMR5 Link Image
Enzyme 6 GenAtlas ID SARDH Link Image
Enzyme 6 HGNC ID HGNC:10536 Link Image
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 17179
Enzyme 7 Name Proton-coupled amino acid transporter 2
Enzyme 7 Synonyms
  1. Proton/amino acid transporter 2
  2. Solute carrier family 36 member 2
  3. Tramdorin-1
Enzyme 7 Gene Name SLC36A2
Enzyme 7 Protein Sequence >Proton-coupled amino acid transporter 2
MSVTKSTEGPQGAVAIKLDLMSPPESAKKLENKDSTFLDESPSESAGLKKTKGITVFQAL
IHLVKGNMGTGILGLPLAVKNAGILMGPLSLLVMGFIACHCMHILVKCAQRFCKRLNKPF
MDYGDTVMHGLEANPNAWLQNHAHWGRHIVSFFLIITQLGFCCVYIVFLADNLKQVVEAV
NSTTNNCYSNETVILTPTMDSRLYMLSFLPFLVLLVLIRNLRILTIFSMLANISMLVSLV
IIIQYITQEIPDPSRLPLVASWKTYPLFFGTAIFSFESIGVVLPLENKMKNARHFPAILS
LGMSIVTSLYIGMAALGYLRFGDDIKASISLNLPNCWLYQSVKLLYIAGILCTYALQFYV
PAEIIIPFAISRVSTRWALPLDLSIRLVMVCLTCLLAILIPRLDLVISLVGSVSGTALAL
IIPPLLEVTTFYSEGMSPLTIFKDALISILGFVGFVVGTYQALDELLKSEDSHPFSNSTT
FVR
Enzyme 7 Number of Residues 483
Enzyme 7 Molecular Weight 53215.7
Enzyme 7 Theoretical pI 8.20
Enzyme 7 GO Classification Not Available
Enzyme 7 General Function Amino acid transport and metabolism
Enzyme 7 Specific Function Involved in a pH-dependent electrogenic neuronal transport and sequestration of small amino acids amino acids such as glycine, alanine and proline. Inhibited by sarcosine
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • 59-79 82-102 149-169 198-218 223-243 265-285 297-317 350-370 380-400 405-425 438-458
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 34527813 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q495M3 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name S36A2_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1452 bp
ATGTCTGTGACAAAAAGTACTGAGGGTCCCCAGGGAGCCGTTGCCATCAAATTGGACCTT
ATGTCGCCTCCTGAAAGTGCCAAGAAGTTGGAGAACAAGGACTCTACATTCTTGGATGAA
AGTCCTTCAGAGTCAGCAGGCTTGAAGAAGACCAAGGGCATAACAGTGTTCCAGGCCTTG
ATTCACCTGGTGAAAGGCAACATGGGCACAGGGATCCTGGGACTACCCCTCGCTGTGAAG
AACGCGGGCATCCTGATGGGCCCACTCAGTCTGCTGGTGATGGGCTTCATTGCCTGCCAC
TGTATGCACATCCTGGTCAAGTGTGCCCAGCGCTTCTGTAAGAGGCTTAACAAGCCCTTT
ATGGACTATGGGGACACGGTGATGCATGGACTAGAAGCCAACCCCAACGCCTGGCTCCAG
AATCACGCTCACTGGGGAAGGCATATCGTGAGCTTCTTCCTTATTATCACCCAACTTGGC
TTCTGCTGTGTGTACATTGTGTTTTTGGCTGATAATTTAAAACAGGTAGTGGAAGCTGTT
AATAGCACAACCAACAACTGCTATTCCAATGAGACGGTGATTCTGACCCCCACCATGGAC
TCGCGACTCTACATGCTCTCCTTCCTGCCCTTCCTGGTGCTGCTGGTCCTCATCCGGAAC
CTCAGGATCTTGACCATCTTCTCCATGCTGGCCAACATCAGCATGCTGGTCAGCTTGGTC
ATCATCATACAGTACATTACCCAGGAAATCCCAGACCCCAGCCGGTTGCCACTGGTAGCA
AGCTGGAAGACCTACCCTCTCTTCTTCGGAACAGCCATTTTTTCTTTTGAAAGCATTGGT
GTGGTTCTGCCTCTGGAAAACAAGATGAAGAATGCCCGCCACTTCCCAGCCATCCTGTCT
TTGGGAATGTCCATCGTCACTTCCCTATACATTGGCATGGCGGCTCTGGGCTACCTGCGG
TTTGGAGATGACATCAAGGCCAGCATAAGCCTTAACCTGCCTAACTGCTGGCTGTACCAG
TCTGTCAAGCTTCTCTACATTGCCGGCATCCTGTGCACCTATGCCCTGCAGTTCTACGTC
CCTGCAGAAATCATCATCCCCTTTGCCATCTCCCGGGTGTCAACACGCTGGGCACTGCCT
CTGGATCTGTCCATTCGCCTCGTCATGGTCTGCCTGACATGCCTCCTGGCCATCCTCATC
CCCCGCCTGGACCTGGTCATCTCCCTGATGGGCTCCGTGAGTGGCACCGCCCTGGCCCTC
ATCATCCCACCGCTCCTGGAGGTCCCCACGTTCTACTCAGAGGGCATGAGCCCCCTCACC
ATCTTCAAGGACGCCCTGATCAGCATCCTGGGCTTCGTGGGCTTTGTGGTGGGGACCTAC
CAGGCCCTGGACGAGCTGCTCAAGTCAGAAGACTCTCACCCCTTTTCCAACTCCACCACT
TTTGTTCGGTGA
Enzyme 7 GenBank Gene ID AK122630 Link Image
Enzyme 7 GeneCard ID SLC36A2 Link Image
Enzyme 7 GenAtlas ID SLC36A2 Link Image
Enzyme 7 HGNC ID HGNC:18762 Link Image
Enzyme 7 Chromosome Location 5
Enzyme 7 Locus 5q33.1
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Boll M, Foltz M, Rubio-Aliaga I, Daniel H: A cluster of proton/amino acid transporter genes in the human and mouse genomes. Genomics. 2003 Jul;82(1):47-56. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Bermingham JR Jr, Pennington J: Organization and expression of the SLC36 cluster of amino acid transporter genes. Mamm Genome. 2004 Feb;15(2):114-25. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available