| Version |
2.5 |
| Creation Date |
2005-11-16 15:48:42 |
| Update Date |
2010-04-21 22:53:16 |
| Accession Number |
HMDB00092 |
| Secondary Accession Numbers |
Not Available |
| Common Name |
Dimethylglycine |
| Description |
Dimethylglycine (DMG) is an amino acid derivative found in the cells of all plants and animals and can be obtained in the diet in small amounts from grains and meat. The human body produces DMG when metabolizing choline into Glycine. Dimethylglycine that is not metabolized in the liver is transported by the circulatory system to body tissue. Dimethylglycine was popular with Russian athletes and cosmonauts owing to its reputed ability to increase endurance and reduce fatigue. DMG is also a byproduct of homocysteine metabolism. Homocysteine and betaine are converted to methionine and N, N-dimethylglycine by betaine-homocysteine methyltransferase. |
| Synonyms |
- (Dimethylamino)acetate
- (Dimethylamino)acetic acid
- 2-(Dimethylamino)acetate
- 2-(Dimethylamino)acetic acid
- Dimethylglycine
- N,N-Dimethylaminoacetate
- N,N-Dimethylaminoacetic acid
- N,N-Dimethylglycine
- N-Methylsarcosine N,N-dimethyl-Glycine
|
| Chemical IUPAC Name |
2-dimethylaminoacetic acid |
| Chemical Formula |
C4H9NO2 |
| Chemical Structure |
 |
| Chemical Taxonomy |
| Kingdom |
|
| Super Class |
- Amino acids and Amino Acid conjugates
|
| Class |
|
| Sub Class |
|
| Family |
|
| Species |
- tertiary amine
- tertiary aliphatic amine (trialkylamine)
- carboxylic acid
|
| Biofunction |
- Component of Glycine, serine and threonine metabolism
- Component of Methionine metabolism
|
| Application |
| — |
| Source |
|
|
| Average Molecular Weight |
103.120 |
| Monoisotopic Molecular Weight |
103.063332 |
| Isomeric SMILES |
CN(C)CC(O)=O |
| Canonical SMILES |
CN(C)CC(O)=O |
| KEGG Compound ID |
C01026  |
| BioCyc ID |
DIMETHYL-GLYCINE  |
| BiGG ID |
36652  |
| Wikipedia Link |
Dimethylglycine  |
| NuGOwiki Link |
HMDB00092  |
| Metagene Link |
HMDB00092  |
| METLIN ID |
277  |
| PubChem Compound |
673  |
| PubChem Substance |
6436203  |
| ChEBI ID |
17724  |
| CAS Registry Number |
1118-68-9 |
| InChI Identifier |
InChI=1/C4H9NO2/c1-5(2)3-4(6)7/h3H2,1-2H3,(H,6,7) |
| Synthesis Reference |
Lai, Mei-Chin; Wang, Chia-Chi; Chuang, Ming-Jen; Wu, Yen-Chi; Lee, Yu-Chien. Effects of substrate and potassium on the betaine-synthesizing enzyme glycine sarcosine dimethylglycine N-methyltransferase from a halophilic methanoarchaeon Methanohalophilus po |
| Melting Point (Experimental) |
185.5 oC |
| Experimental Water Solubility |
Not Available
Source: PhysProp
|
| Predicted Water Solubility |
298.0 mg/mL [MEYLAN,WM et al. (1996)]; 939.00006 mg/mL [Predicted by ALOGPS]
Calculated using ALOGPS
|
| Physiological Charge |
0 |
| State |
Solid |
| Experimental LogP/Hydrophobicity |
-2.91 [TSAI,RS ET AL. (1991)]
Source: PhysProp
|
| Predicted LogP/Hydrophobicity |
-1.70 [Predicted by ALOGPS]; -0.6 [Predicted by PubChem via XLOGP]
Calculated using ALOGPS
|
| Material Safety Data Sheet (MSDS) |
|
| MOL File |
Show  |
| SDF File |
Show  |
| PDB File |
Show  |
| 2D Structure |
|
| 3D Structure |
|
| Experimental PDB ID |
1EL5  |
| Experimental PDB File |
Show |
| Experimental PDB Structure |
|
| Experimental 1H NMR Spectrum |
Download Spectrum Download FID (Varian) Show Experimental Conditions  |
| Experimental 13C NMR Spectrum |
Download Spectrum Download FID (Bruker) Show Experimental Conditions  |
| Experimental 13C HSQC Spectrum |
Download Spectrum Download FID (Bruker) Show Experimental Conditions  |
| Predicted 1H NMR Spectrum |
Show Image Show Peaklist
|
| Predicted 13C NMR Spectrum |
Show Image Show Peaklist
|
| Mass Spectrum |
|
| Simplified TOCSY Spectrum |
Not Available |
| BMRB Spectrum |
Show Image Show Peaklist |
| Cellular Location |
|
| Biofluid Location |
|
| Tissue Location |
| Tissue |
References |
| Kidney |
— |
| Liver |
— |
|
| Concentrations (Normal) |
| Biofluid |
Blood |
| Value |
2.6 (1.8-3.7) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- McGregor DO, Dellow WJ, Lever M, George PM, Robson RA, Chambers ST: Dimethylglycine accumulates in uremia and predicts elevated plasma homocysteine concentrations. Kidney Int. 2001 Jun;59(6):2267-72. [PubMed
]
|
| Biofluid |
Blood |
| Value |
1.9 (1.1-3.4) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Lever M, George PM, Dellow WJ, Scott RS, Chambers ST: Homocysteine, glycine betaine, and N,N-dimethylglycine in patients attending a lipid clinic. Metabolism. 2005 Jan;54(1):1-14. [PubMed
]
|
| Biofluid |
Urine |
| Value |
3.4 (0.7-10.6) umol/mmol creatinine |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Lever M, George PM, Dellow WJ, Scott RS, Chambers ST: Homocysteine, glycine betaine, and N,N-dimethylglycine in patients attending a lipid clinic. Metabolism. 2005 Jan;54(1):1-14. [PubMed
]
|
| Biofluid |
Urine |
| Value |
6.2 (0.8-11.2) umol/mmol creatinine |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Laryea MD, Steinhagen F, Pawliczek S, Wendel U: Simple method for the routine determination of betaine and N,N-dimethylglycine in blood and urine. Clin Chem. 1998 Sep;44(9):1937-41. [PubMed
]
|
|
| Concentrations (Abnormal) |
| Biofluid |
Blood |
| Value |
4.8 (3.6-6.2) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Kidney disease |
| Comments |
Patients with chronic renal failure who were not receiving dialysis |
| References |
- McGregor DO, Dellow WJ, Lever M, George PM, Robson RA, Chambers ST: Dimethylglycine accumulates in uremia and predicts elevated plasma homocysteine concentrations. Kidney Int. 2001 Jun;59(6):2267-72. [PubMed
]
|
| Biofluid |
Blood |
| Value |
5.4 (3.1-7.2) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Kidney disease |
| Comments |
Patient group: various renal conditions with chronic ambulatory peritoneal dialysis |
| References |
- McGregor DO, Dellow WJ, Lever M, George PM, Robson RA, Chambers ST: Dimethylglycine accumulates in uremia and predicts elevated plasma homocysteine concentrations. Kidney Int. 2001 Jun;59(6):2267-72. [PubMed
]
|
| Biofluid |
Blood |
| Value |
5.6 (4.8 - 10.1) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Kidney disease |
| Comments |
Patients with various renal conditions on long-term (>6 months) hemodialysis |
| References |
- McGregor DO, Dellow WJ, Lever M, George PM, Robson RA, Chambers ST: Dimethylglycine accumulates in uremia and predicts elevated plasma homocysteine concentrations. Kidney Int. 2001 Jun;59(6):2267-72. [PubMed
]
|
|
| Associated Disorders |
| Condition |
References |
| Kidney disease |
- McGregor DO, Dellow WJ, Lever M, George PM, Robson RA, Chambers ST: Dimethylglycine accumulates in uremia and predicts elevated plasma homocysteine concentrations. Kidney Int. 2001 Jun;59(6):2267-72. [PubMed
]
|
|
| OMIM ID |
Not Available |
| Pathways |
|
| General References |
- 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
]
- McGregor DO, Dellow WJ, Lever M, George PM, Robson RA, Chambers ST: Dimethylglycine accumulates in uremia and predicts elevated plasma homocysteine concentrations. Kidney Int. 2001 Jun;59(6):2267-72. [PubMed
]
- 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
]
- Look MP, Riezler R, Reichel C, Brensing KA, Rockstroh JK, Stabler SP, Spengler U, Berthold HK, Sauerbruch T: Is the increase in serum cystathionine levels in patients with liver cirrhosis a consequence of impaired homocysteine transsulfuration at the level of gamma-cystathionase? Scand J Gastroenterol. 2000 Aug;35(8):866-72. [PubMed
]
- Cicek G, Vuorinen T, Stahle I, Stepanek P, Freudenberg N, Brandsch R: Coxsackievirus B3 infection induces anti-flavoprotein antibodies in mice. Clin Exp Immunol. 2000 Dec;122(3):404-9. [PubMed
]
- Lever M, George PM, Dellow WJ, Scott RS, Chambers ST: Homocysteine, glycine betaine, and N,N-dimethylglycine in patients attending a lipid clinic. Metabolism. 2005 Jan;54(1):1-14. [PubMed
]
- Xia JH, Yu KP, Liu CY, Pan Q, Zheng D, Dai HP: [Molecular clonging of the human dimethyglycine dehydrogenase-like gene (DMGDHL1) from the sarcosinemia critical region at 9q34] Yi Chuan Xue Bao. 1999;26(6):591-7. [PubMed
]
- Laryea MD, Steinhagen F, Pawliczek S, Wendel U: Simple method for the routine determination of betaine and N,N-dimethylglycine in blood and urine. Clin Chem. 1998 Sep;44(9):1937-41. [PubMed
]
- 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
]
- Jansen M, Hansen TA: Non-growth-associated demethylation of dimethylsulfoniopropionate by (homo)acetogenic bacteria. Appl Environ Microbiol. 2001 Jan;67(1):300-6. [PubMed
]
- Wikipedia

|
| Metabolic Enzymes |
- Dimethylglycine dehydrogenase, mitochondrial
- Betaine--homocysteine S-methyltransferase 1
- Betaine--homocysteine S-methyltransferase 2
|
|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5435 |
| Enzyme 1 Name |
Dimethylglycine dehydrogenase, mitochondrial |
| Enzyme 1 Synonyms |
- ME2GLYDH
|
| Enzyme 1 Gene Name |
DMGDH |
| Enzyme 1 Protein Sequence |
>Dimethylglycine dehydrogenase, mitochondrial
MLRPGAQLLRGLLLRSCPLQGSPGRPRSVCGREGEEKPPLSAETQWKDRAETVIIGGGCV
GVSLAYHLAKAGMKDVVLLEKSELTAGSTWHAAGLTTYFHPGINLKKIHYDSIKLYEKLE
EETGQVVGFHQPGSIRLATTPVRVDEFKYQMTRTGWHATEQYLIEPEKIQEMFPLLNMNK
VLAGLYNPGDGHIDPYSLTMALAAGARKCGALLKYPAPVTSLKARSDGTWDVETPQGSMR
ANRIVNAAGFWAREVGKMIGLEHPLIPVQHQYVVTSTISEVKALKRELPVLRDLEGSYYL
RQERDGLLFGPYESQEKMKVQDSWVTNGVPPGFGKELFESDLDRIMEHIKAAMEMVPVLK
KADIINVVNGPITYSPDILPMVGPHQGVRNYWVAIGFGYGIIHAGGVGKYLSDWILHGEP
PFDLIELDPNRYGKWTTTQYTEAKARESYGFNNIVGYPKEERFAGRPTQRVSGLYQRLES
KCSMGFHAGWEQPHWFYKPGQDTQYRPSFRRTNWFEPVGSEYKQVMQRVAVTDLSPFGKF
NIKGQDSIRLLDHLFANVIPKVGFTNISHMLTPKGRVYAELTVSHQSPGEFLLITGSGSE
LHDLRWIEEEAVKGGYDVEIKNITDELGVLGVAGPQARKVLQKLTSEDLSDDVFKFLQTK
SLKVSNIPVTAIRISYTGELGWELYHRREDSVALYDAIMNAGQEEGIDNFGTYAMNALRL
EKAFRAWGLEMNCDTNPLEAGLEYFVKLNKPADFIGKQALKQIKAKGLKRRLVCLTLATD
DVDPEGNESIWYNGKVVGNTTSGSYSYSIQKSLAFAYVPVQLSEVGQQVEVELLGKNYPA
VIIQEPLVLTEPTRNRLQKKGGKDKT
|
| Enzyme 1 Number of Residues |
866 |
| Enzyme 1 Molecular Weight |
96810.1 |
| Enzyme 1 Theoretical pI |
7.69 |
| Enzyme 1 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 1 General Function |
Involved in oxidoreductase activity |
| Enzyme 1 Specific Function |
N,N-dimethylglycine + acceptor + H(2)O = sarcosine + formaldehyde + reduced acceptor |
| Enzyme 1 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 1 Reactions |
- N,N-dimethylglycine + acceptor + H2O = sarcosine + formaldehyde + reduced acceptor [RN:R01565]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
24797151  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q9UI17  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
M2GD_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 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 1 GenBank Gene ID |
NM_013391.2  |
| Enzyme 1 GeneCard ID |
DMGDH  |
| Enzyme 1 GenAtlas ID |
DMGDH  |
| Enzyme 1 HGNC ID |
HGNC:24475  |
| Enzyme 1 Chromosome Location |
5 |
| Enzyme 1 Locus |
5q14.1 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5831 |
| Enzyme 2 Name |
Betaine--homocysteine S-methyltransferase 1 |
| Enzyme 2 Synonyms |
Not Available |
| Enzyme 2 Gene Name |
BHMT |
| Enzyme 2 Protein Sequence |
>Betaine--homocysteine S-methyltransferase 1
MPPVGGKKAKKGILERLNAGEIVIGDGGFVFALEKRGYVKAGPWTPEAAVEHPEAVRQLH
REFLRAGSNVMQTFTFYASEDKLENRGNYVLEKISGQEVNEAACDIARQVADEGDALVAG
GVSQTPSYLSCKSETEVKKVFLQQLEVFMKKNVDFLIAEYFEHVEEAVWAVETLIASGKP
VAATMCIGPEGDLHGVPPGECAVRLVKAGASIIGVNCHFDPTISLKTVKLMKEGLEAARL
KAHLMSQPLAYHTPDCNKQGFIDLPEFPFGLEPRVATRWDIQKYAREAYNLGVRYIGGCC
GFEPYHIRAIAEELAPERGFLPPASEKHGSWGSGLDMHTKPWVRARARKEYWENLRIASG
RPYNPSMSKPDGWGVTKGTAELMQQKEATTEQQLKELFEKQKFKSQ
|
| Enzyme 2 Number of Residues |
406 |
| Enzyme 2 Molecular Weight |
44998.2 |
| Enzyme 2 Theoretical pI |
7.04 |
| Enzyme 2 GO Classification |
| Function |
- S-methyltransferase activity
- betaine-homocysteine S-methyltransferase activity
- binding
- catalytic activity
- cation binding
- homocysteine S-methyltransferase activity
- ion binding
- metal ion binding
- methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
- transition metal ion binding
- zinc ion binding
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
- methionine biosynthetic process
- sulfur amino acid biosynthetic process
- sulfur amino acid metabolic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 2 General Function |
Involved in zinc ion binding |
| Enzyme 2 Specific Function |
Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline |
| Enzyme 2 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
- Methionine Metabolism (map00271
)
|
| Enzyme 2 Reactions |
- trimethylammonioacetate + L-homocysteine = dimethylglycine + L-methionine [RN:R02821]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
4530461  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q93088  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
BHMT1_HUMAN  |
| Enzyme 2 PDB ID |
1LT8  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1221 bp
ATGCCACCCGTTGGGGGCAAAAAGGCCAAGAAGGGCATCCTAGAACGTTTAAATGCTGGA
GAGATTGTGATTGGAGATGGAGGGTTTGTCTTTGCACTGGAGAAGAGGGGCTACGTAAAG
GCAGGACCCTGGACTCCTGAAGCTGCTGTGGAGCACCCAGAAGCAGTTCGCCAGCTTCAT
CGAGAGTTCCTCAGAGCTGGCTCAAACGTCATGCAGACCTTCACCTTCTATGCGAGTGAA
GACAAGCTGGAGAACAGGGGCAACTATGTCTTAGAGAAGATATCTGGGCAGGAAGTCAAT
GAAGCTGCTTGCGACATCGCCCGACAAGTGGCTGATGAAGGAGATGCTTTGGTAGCAGGA
GGAGTGAGTCAGACACCTTCATACCTTAGCTGCAAGAGTGAAACTGAAGTCAAAAAAGTA
TTTCTGCAACAGTTAGAGGTCTTTATGAAGAAGAACGTGGACTTCTTGATTGCAGAGTAT
TTTGAACACGTTGAAGAAGCTGTGTGGGCAGTTGAAACCTTGATAGCATCCGGTAAACCT
GTGGCAGCAACCATGTGCATTGGCCCAGAAGGAGATTTGCATGGCGTGCCCCCCGGCGAG
TGTGCAGTGCGCCTGGTGAAAGCAGGAGCATCCATCATTGGTGTGAACTGCCACTTTGAC
CCCACCATTAGTTTAAAAACAGTGAAGCTCATGAAGGAGGGCTTGGAGGCTGCCCGACTG
AAAGCTCACCTGATGAGCCAGCCCTTGGCTTACCACACTCCTGACTGCAACAAGCAGGGA
TTCATCGATCTCCCAGAATTCCCATTTGGACTGGAACCCAGAGTTGCCACCAGATGGGAT
ATTCAAAAATACGCCAGAGAGGCCTACAACCTGGGGGTCAGGTACATTGGCGGGTGCTGT
GGATTTGAGCCCTACCACATCAGGGCAATTGCAGAGGAGCTGGCCCCAGAAAGGGGCTTT
TTGCCACCAGCTTCAGAAAAACATGGCAGCTGGGGAAGTGGTTTGGACATGCACACCAAA
CCCTGGGTTAGAGCAAGGGCCAGGAAGGAATACTGGGAGAATCTTCGGATAGCCTCAGGC
CGGCCATACAACCCTTCAATGTCAAAGCCAGATGGCTGGGGAGTGACCAAAGGAACAGCC
GAGCTGATGCAGCAGAAAGAAGCCACAACTGAGCAGCAGCTGAAAGAGCTCTTTGAAAAA
CAAAAATTCAAATCACAGTAG
|
| Enzyme 2 GenBank Gene ID |
AF118378  |
| Enzyme 2 GeneCard ID |
BHMT  |
| Enzyme 2 GenAtlas ID |
BHMT  |
| Enzyme 2 HGNC ID |
HGNC:1047  |
| Enzyme 2 Chromosome Location |
5 |
| Enzyme 2 Locus |
5q13.1-q15 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Garrow TA: Purification, kinetic properties, and cDNA cloning of mammalian betaine-homocysteine methyltransferase. J Biol Chem. 1996 Sep 13;271(37):22831-8. [PubMed
]
- Park EI, Garrow TA: Interaction between dietary methionine and methyl donor intake on rat liver betaine-homocysteine methyltransferase gene expression and organization of the human gene. J Biol Chem. 1999 Mar 19;274(12):7816-24. [PubMed
]
- 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
]
- Sunden SL, Renduchintala MS, Park EI, Miklasz SD, Garrow TA: Betaine-homocysteine methyltransferase expression in porcine and human tissues and chromosomal localization of the human gene. Arch Biochem Biophys. 1997 Sep 1;345(1):171-4. [PubMed
]
- Millian NS, Garrow TA: Human betaine-homocysteine methyltransferase is a zinc metalloenzyme. Arch Biochem Biophys. 1998 Aug 1;356(1):93-8. [PubMed
]
- Evans JC, Huddler DP, Jiracek J, Castro C, Millian NS, Garrow TA, Ludwig ML: Betaine-homocysteine methyltransferase: zinc in a distorted barrel. Structure. 2002 Sep;10(9):1159-71. [PubMed
]
- Weisberg IS, Park E, Ballman KV, Berger P, Nunn M, Suh DS, Breksa AP 3rd, Garrow TA, Rozen R: Investigations of a common genetic variant in betaine-homocysteine methyltransferase (BHMT) in coronary artery disease. Atherosclerosis. 2003 Apr;167(2):205-14. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
9885 |
| Enzyme 3 Name |
Betaine--homocysteine S-methyltransferase 2 |
| Enzyme 3 Synonyms |
Not Available |
| Enzyme 3 Gene Name |
BHMT2 |
| Enzyme 3 Protein Sequence |
>Betaine--homocysteine S-methyltransferase 2
MAPAGRPGAKKGILERLESGEVVIGDGSFLITLEKRGYVKAGLWTPEAVIEHPDAVRQLH
MEFLRAGSNVMQTFTFSASEDNMESKWEDVNAAACDLAREVAGKGDALVAGGICQTSIYK
YQKDEARIKKLFRQQLEVFAWKNVDFLIAEYFEHVEEAVWAVEVLKESDRPVAVTMCIGP
EGDMHDITPGECAVRLVKAGASIVGVNCRFGPDTSLKTMELMKEGLEWAGLKAHLMVQPL
GFHAPDCGKEGFVDLPEYPFGLESRVATRWDIQKYAREAYNLGVRYIGGCCGFEPYHIRA
IAEELAPERGFLPPASEKHGSWGSGLDMHTKPWIRARARREYWENLLPASGRPFCPSLSK
PDF
|
| Enzyme 3 Number of Residues |
363 |
| Enzyme 3 Molecular Weight |
40353.8 |
| Enzyme 3 Theoretical pI |
5.68 |
| Enzyme 3 GO Classification |
| Function |
- S-methyltransferase activity
- betaine-homocysteine S-methyltransferase activity
- binding
- catalytic activity
- cation binding
- homocysteine S-methyltransferase activity
- ion binding
- metal ion binding
- methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
- transition metal ion binding
- zinc ion binding
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
- methionine biosynthetic process
- sulfur amino acid biosynthetic process
- sulfur amino acid metabolic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 3 General Function |
Involved in zinc ion binding |
| Enzyme 3 Specific Function |
Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline |
| Enzyme 3 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
- Methionine Metabolism (map00271
)
|
| Enzyme 3 Reactions |
- trimethylammonioacetate + L-homocysteine = dimethylglycine + L-methionine [RN:R02821]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
11907831  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q9H2M3  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
BHMT2_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1092 bp
ATGGCACCTGCTGGACGCCCGGGGGCCAAGAAGGGGATTTTGGAGCGCCTGGAGAGTGGG
GAGGTTGTGATTGGAGATGGCAGCTTTCTCATTACTCTGGAGAAGAGAGGCTATGTGAAG
GCTGGGCTCTGGACTCCAGAGGCAGTGATAGAACACCCAGACGCAGTTCGTCAACTTCAC
ATGGAATTCTTGAGAGCAGGATCAAATGTCATGCAGACTTTTACCTTTTCTGCCAGTGAG
GACAATATGGAAAGCAAGTGGGAAGATGTAAATGCTGCTGCCTGTGACCTCGCCAGGGAA
GTGGCTGGCAAAGGTGATGCTTTGGTAGCAGGGGGGATCTGCCAGACATCAATATACAAA
TACCAGAAGGATGAAGCTAGAATTAAAAAACTTTTTCGACAACAGCTAGAAGTTTTTGCC
TGGAAAAATGTGGACTTCTTGATTGCAGAGTATTTTGAGCACGTTGAAGAAGCTGTGTGG
GCTGTGGAAGTCTTAAAAGAATCAGATAGACCCGTGGCAGTTACCATGTGCATAGGCCCA
GAGGGAGACATGCATGATATAACCCCCGGAGAATGTGCTGTGAGGCTGGTGAAGGCAGGG
GCTTCCATCGTTGGCGTGAACTGCCGCTTTGGGCCCGACACCAGCTTGAAGACGATGGAG
CTCATGAAGGAGGGTCTTGAGTGGGCAGGGCTGAAAGCGCACCTCATGGTGCAGCCTCTG
GGGTTCCACGCGCCTGACTGTGGCAAAGAGGGGTTTGTGGATCTCCCAGAATATCCCTTT
GGACTGGAGTCCAGAGTTGCCACCAGATGGGATATTCAAAAATACGCCAGAGAGGCCTAC
AACCTGGGGGTCAGGTACATTGGCGGGTGCTGTGGATTTGAGCCCTACCACATCAGGGCA
ATTGCAGAGGAGCTGGCCCCAGAAAGGGGCTTTTTGCCACCAGCTTCAGAAAAACACGGC
AGCTGGGGAAGTGGTTTGGACATGCACACCAAACCCTGGATTAGAGCAAGGGCTCGAAGG
GAGTATTGGGAGAATCTGCTGCCAGCTTCAGGCAGACCTTTCTGTCCTTCGCTGTCAAAG
CCAGACTTCTAA
|
| Enzyme 3 GenBank Gene ID |
AF257473  |
| Enzyme 3 GeneCard ID |
BHMT2  |
| Enzyme 3 GenAtlas ID |
BHMT2  |
| Enzyme 3 HGNC ID |
HGNC:1048  |
| Enzyme 3 Chromosome Location |
5 |
| Enzyme 3 Locus |
5q13 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Chadwick LH, McCandless SE, Silverman GL, Schwartz S, Westaway D, Nadeau JH: Betaine-homocysteine methyltransferase-2: cDNA cloning, gene sequence, physical mapping, and expression of the human and mouse genes. Genomics. 2000 Nov 15;70(1):66-73. [PubMed
]
- 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
]
- 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
]
|
| Enzyme 3 Metabolite References |
Not Available |