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Human Metabolome Database Version 2.5

 

Showing metabocard for D-Lactic acid (HMDB01311)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2011-03-09 17:11:46
Accession Number HMDB01311
Secondary Accession Numbers HMDB00171
Common Name D-Lactic acid
Description D-Lactic acid is the end product of the enzyme Glyoxalase II ([EC:3.1.2.6] hydroxyacyl-glutathione hydrolase) which converts the intermediate substrate S-lactoyl-glutathione to reduced glutathione and D-lactate. (OMIM 138790)
Synonyms
  1. (-)-Lactate
  2. (-)-Lactic acid
  3. (R)-(-)-Lactate
  4. (R)-(-)-Lactic acid
  5. (R)-2-Hydroxypropanoate
  6. (R)-2-Hydroxypropanoic acid
  7. (R)-2-Hydroxypropionate
  8. (R)-2-Hydroxypropionic acid
  9. (R)-Lactate
  10. (R)-Lactic acid
  11. (R)-a-Hydroxypropionate
  12. (R)-a-Hydroxypropionic acid
  13. (R)-alpha-Hydroxypropionate
  14. (R)-alpha-Hydroxypropionic acid
  15. D-(-)-Lactate
  16. D-(-)-Lactic acid
  17. D-2-Hydroxypropanoate
  18. D-2-Hydroxypropanoic acid
  19. D-2-Hydroxypropionate
  20. D-2-Hydroxypropionic acid
  21. D-Lactate
  22. D-Lactic acid
  23. DLA
  24. L-(+)-Lactate
  25. L-Lactic acid
  26. Propel
  27. Tisulac
  28. delta-(-)-Lactate
  29. delta-(-)-Lactic acid
  30. delta-2-Hydroxypropanoate
  31. delta-2-Hydroxypropanoic acid
  32. delta-2-Hydroxypropionate
  33. delta-2-Hydroxypropionic acid
  34. delta-Lactate
  35. delta-Lactic acid
Chemical IUPAC Name (2R)-2-hydroxypropanoic acid
Chemical Formula C3H6O3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Hydroxy Acids
Sub Class
  • Short chain hydroxy acids
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • carboxylic acid
  • alpha-hydroxyacid
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 90.078
Monoisotopic Molecular Weight 90.031693
Isomeric SMILES C[C@@H](O)C(O)=O
Canonical SMILES CC(O)C(O)=O
KEGG Compound ID C00256 Link Image
BioCyc ID D-LACTATE Link Image
BiGG ID 34414 Link Image
Wikipedia Link DLA Link Image
NuGOwiki Link HMDB01311 Link Image
Metagene Link HMDB01311 Link Image
METLIN ID 6150 Link Image
PubChem Compound 61503 Link Image
PubChem Substance 8187556 Link Image
ChEBI ID 341 Link Image
CAS Registry Number 10326-41-7
InChI Identifier InChI=1/C3H6O3/c1-2(4)3(5)6/h2,4H,1H3,(H,5,6)/t2-/m1/s1
Synthesis Reference Hsieh, Chun Lung; Houng, Jer Yiing. Preparation of D-lactic acid from D,L-lactic acid ester using wheat germ or pancreatic lipase. U.S. (1997), 5 pp.
Melting Point (Experimental) 52.8 C
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1000.0 mg/mL [MEYLAN,WM et al. (1996)]; 562.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.79 [Predicted by ALOGPS]; -0.6 [Predicted by PubChem via XLOGP]; -0.65 [MEYLAN,WM & HOWARD,PH (1995)] 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 Not Available
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 Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • Extracellular
  • mitochondria
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Bladder
Brain
Fibroblasts
Gut
Intestine
Liver
Muscle
Neuron
Placenta
Platelet
Skeletal Muscle
Skin
Spleen
Stratum Corneum
Testes
Concentrations (Normal)
Biofluid Blood
Value 11.0 +/- 1.2 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • McLellan AC, Phillips SA, Thornalley PJ: Fluorimetric assay of D-lactate. Anal Biochem. 1992 Oct;206(1):12-6. [PubMed Link Image]
Biofluid Urine
Value 23.00 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Concentrations (Abnormal)
Biofluid Blood
Value 20.0 +/- 1.3 uM
Age Adult:>18 yrs old
Sex Both
Condition Diabetes mellitus type 2
Comments Not Available
References
  • McLellan AC, Phillips SA, Thornalley PJ: Fluorimetric assay of D-lactate. Anal Biochem. 1992 Oct;206(1):12-6. [PubMed Link Image]
Biofluid CSF
Value >2300 uM
Age Children:1-13 yrs old
Sex N/A
Comments Not Available
References
  • Zeman J, Stratilova L, Houst'kova H, Dudkova Z, Hansikova H, Konradova V, Hruba E, Hoza J, Zeman L: [Lactate acidosis in childhood]. Cas Lek Cesk. 1998 Sep 21;137(18):557-60. [PubMed Link Image]
Associated Disorders
Condition References
Diabetes mellitus type 2
  • McLellan AC, Phillips SA, Thornalley PJ: Fluorimetric assay of D-lactate. Anal Biochem. 1992 Oct;206(1):12-6. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Pyruvaldehyde Degradation SMP00459 Link Image
Pyruvate Metabolism SMP00060 Link Image map00620 Link Image
General References
  1. Hasegawa H, Fukushima T, Lee JA, Tsukamoto K, Moriya K, Ono Y, Imai K: Determination of serum D-lactic and L-lactic acids in normal subjects and diabetic patients by column-switching HPLC with pre-column fluorescence derivatization. Anal Bioanal Chem. 2003 Nov;377(5):886-91. Epub 2003 Jul 19. [PubMed Link Image]
  2. Smith SM, Eng RH, Buccini F: Use of D-lactic acid measurements in the diagnosis of bacterial infections. J Infect Dis. 1986 Oct;154(4):658-64. [PubMed Link Image]
  3. Ellis LC, Groesbeck MD, Farr CH, Tesi RJ: Contractility of seminiferous tubules as related to sperm transport in the male. Arch Androl. 1981 Jun;6(4):283-94. [PubMed Link Image]
  4. Pedersen M: Ciliary activity and pollution. Lung. 1990;168 Suppl:368-76. [PubMed Link Image]
  5. McLellan AC, Phillips SA, Thornalley PJ: Fluorimetric assay of D-lactate. Anal Biochem. 1992 Oct;206(1):12-6. [PubMed Link Image]
  6. Schmid-Schonbein GW: Microlymphatics and lymph flow. Physiol Rev. 1990 Oct;70(4):987-1028. [PubMed Link Image]
  7. Solito R, Alessandrini C, Fruschelli M, Pucci AM, Gerli R: An immunological correlation between the anchoring filaments of initial lymph vessels and the neighboring elastic fibers: a unified morphofunctional concept. Lymphology. 1997 Dec;30(4):194-202. [PubMed Link Image]
  8. Brandt RB, Siegel SA: Methylglyoxal production in human blood. Ciba Found Symp. 1978;(67):211-23. [PubMed Link Image]
  9. Zhang YJ, O'Neal WK, Randell SH, Blackburn K, Moyer MB, Boucher RC, Ostrowski LE: Identification of dynein heavy chain 7 as an inner arm component of human cilia that is synthesized but not assembled in a case of primary ciliary dyskinesia. J Biol Chem. 2002 May 17;277(20):17906-15. Epub 2002 Mar 4. [PubMed Link Image]
  10. Tanyel FC, Ulusu NN, Tezcan EF, Buyukpamukcu N: Total calcium content of sacs associated with inguinal hernia, hydrocele or undescended testis reflects differences dictated by programmed cell death. Urol Int. 2003;70(3):211-5. [PubMed Link Image]
  11. Kaneko T, Bando Y, Kurihara H, Satomi K, Nonoyama K, Matsuura N: Fecal microflora in a patient with short-bowel syndrome and identification of dominant lactobacilli. J Clin Microbiol. 1997 Dec;35(12):3181-5. [PubMed Link Image]
  12. Hoijer MA, Melief MJ, van Helden-Meeuwsen CG, Eulderink F, Hazenberg MP: Detection of muramic acid in a carbohydrate fraction of human spleen. Infect Immun. 1995 May;63(5):1652-7. [PubMed Link Image]
  13. Wikipedia Link Image
Metabolic Enzymes
  1. Hydroxyacylglutathione hydrolase, mitochondrial
  2. Probable D-lactate dehydrogenase, mitochondrial
  3. Hydroxyacylglutathione hydrolase-like protein
Enzyme 1 [top]
Enzyme 1 ID 6092
Enzyme 1 Name Hydroxyacylglutathione hydrolase, mitochondrial
Enzyme 1 Synonyms
  1. Glyoxalase II
  2. Glx II
Enzyme 1 Gene Name HAGH
Enzyme 1 Protein Sequence >Hydroxyacylglutathione hydrolase, mitochondrial
MVVGRGLLGRRSLAALGAACARRGLGPALLGVFCHTDLRKNLTVDEGTMKVEVLPALTDN
YMYLVIDDETKEAAIVDPVQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKLESG
LKVYGGDDRIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVSKPGGSEPPAVFT
GDTLFVAGCGKFYEGTADEMCKALLEVLGRLPPDTRVYCGHEYTINNLKFARHVEPGNAA
IREKLAWAKEKYSIGEPTVPSTLAEEFTYNPFMRVREKTVQQHAGETDPVTTMRAVRREK
DQFKMPRD
Enzyme 1 Number of Residues 308
Enzyme 1 Molecular Weight 33805.6
Enzyme 1 Theoretical pI 8.23
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • hydroxyacylglutathione hydrolase activity
  • ion binding
  • metal ion binding
  • thiolester hydrolase activity
  • transition metal ion binding
  • zinc ion binding
Process
Component
Enzyme 1 General Function Involved in hydrolase activity
Enzyme 1 Specific Function Thiolesterase that catalyzes the hydrolysis of S-D- lactoyl-glutathione to form glutathione and D-lactic acid
Enzyme 1 Pathways
Enzyme 1 Reactions
  • S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate [RN:R04090]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 94538322 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q16775 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name GLO2_HUMAN Link Image
Enzyme 1 PDB ID 1QH3 Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >927 bp
ATGGTGGTGGGCCGAGGGCTGCTCGGCCGCCGCAGCCTCGCCGCGCTGGGAGCCGCCTGC
GCCCGCCGAGGCCTCGGTCCAGCCCTGCTGGGAGTTTTCTGCCACACAGATTTGCGGAAG
AACCTGACCGTGGACGAGGGCACCATGAAGGTAGAGGTGCTGCCTGCCCTGACCGACAAC
TACATGTACCTGGTCATTGATGATGAGACCAAGGAGGCTGCCATTGTGGATCCGGTGCAG
CCCCAGAAGGTCGTGGACGCGGCGAGAAAGCACGGGGTGAAACTGACCACAGTGCTCACC
ACCCACCACCACTGGGACCATGCTGGCGGGAATGAGAAACTGGTCAAGCTGGAGTCGGGA
CTGAAGGTGTACGGGGGTGACGACCGTATCGGGGCCCTGACTCACAAGATCACTCACCTG
TCCACACTGCAGGTGGGGTCTCTGAACGTCAAGTGCCTGGCGACCCCGTGCCACACTTCA
GGACACATTTGTTACTTCGTGAGCAAGCCCGGAGGCTCGGAGCCCCCTGCCGTGTTCACA
GGTGACACCTTGTTTGTGGCTGGCTGCGGGAAGTTCTATGAAGGGACTGCGGATGAGATG
TGTAAAGCTCTGCTGGAGGTCTTGGGCCGGCTCCCCCCGGACACAAGAGTCTACTGTGGC
CACGAGTACACCATCAACAACCTCAAGTTTGCACGCCACGTGGAGCCCGGCAATGCCGCC
ATCCGGGAGAAGCTGGCCTGGGCCAAGGAGAAGTACAGCATCGGGGAGCCCACAGTGCCA
TCCACCCTGGCAGAGGAGTTTACCTACAACCCCTTCATGAGAGTGAGGGAGAAGACGGTG
CAGCAGCACGCAGGTGAGACGGACCCGGTGACCACCATGCGGGCCGTGCGCAGGGAGAAG
GACCAGTTCAAGATGCCCCGGGACTGA
Enzyme 1 GenBank Gene ID NM_005326.4 Link Image
Enzyme 1 GeneCard ID HAGH Link Image
Enzyme 1 GenAtlas ID HAGH Link Image
Enzyme 1 HGNC ID HGNC:4805 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 16p13.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. 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]
  2. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
  3. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [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. Ridderstrom M, Saccucci F, Hellman U, Bergman T, Principato G, Mannervik B: Molecular cloning, heterologous expression, and characterization of human glyoxalase II. J Biol Chem. 1996 Jan 5;271(1):319-23. [PubMed Link Image]
  6. Cordell PA, Futers TS, Grant PJ, Pease RJ: The Human hydroxyacylglutathione hydrolase (HAGH) gene encodes both cytosolic and mitochondrial forms of glyoxalase II. J Biol Chem. 2004 Jul 2;279(27):28653-61. Epub 2004 Apr 26. [PubMed Link Image]
  7. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  8. Cameron AD, Ridderstrom M, Olin B, Mannervik B: Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue. Structure. 1999 Sep 15;7(9):1067-78. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 9170
Enzyme 2 Name Probable D-lactate dehydrogenase, mitochondrial
Enzyme 2 Synonyms
  1. DLD
  2. Lactate dehydrogenase D
Enzyme 2 Gene Name LDHD
Enzyme 2 Protein Sequence >Probable D-lactate dehydrogenase, mitochondrial
MARLLRSATWELFPWRGYCSQKAKGELCRDFVEALKAVVGGSHVSTAAVVREQHGRDESV
HRCEPPDAVVWPQNVEQVSRLAALCYRQGVPIIPFGTGTGLEGGVCAVQGGVCVNLTHMD
RILELNQEDFSVVVEPGVTRKALNAHLRDSGLWFPVDPGADASLCGMAATGASGTNAVRY
GTMRDNVLNLEVVLPDGRLLHTAGRGRHFRFGFWPEIPHHTAWYSPCVSLGRRKSAAGYN
LTGLFVGSEGTLGLITATTLRLHPAPEATVAATCAFPSVQAAVDSTVHILQAAVPVARIE
FLDEVMMDACNRYSKLNCLVAPTLFLEFHGSQQALEEQLQRTEEIVQQNGASDFSWAKEA
EERSRLWTARHNAWYAALATRPGCKGYSTDVCVPISRLPEIVVQTKEDLNASGLTGSIVG
HVGDGNFHCILLVNPDDAEELGRVKAFAEQLGRRALALHGTCTGEHGIGMGKRQLLQEEV
GAVGVETMRQLKAVLDPQGLMNPGKVL
Enzyme 2 Number of Residues 507
Enzyme 2 Molecular Weight 54870.2
Enzyme 2 Theoretical pI 6.65
Enzyme 2 GO Classification
Function
  • FAD or FADH2 binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • purine nucleoside binding
Process
Component
Enzyme 2 General Function Involved in catalytic activity
Enzyme 2 Specific Function (R)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c
Enzyme 2 Pathways
Enzyme 2 Reactions
  • (R)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c [RN:R00197]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 37595754 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q86WU2 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name LDHD_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1524 bp
ATGGCCCGACTGCTCAGGTCTGCAACCTGGGAGCTGTTCCCCTGGAGGGGCTACTGCTCC
CAGAAGGCAAAGGGAGAGCTCTGCAGGGACTTCGTAGAGGCTCTGAAGGCCGTGGTGGGC
GGCTCCCACGTGTCCACTGCCGCGGTGGTCCGAGAGCAGCACGGGCGCGATGAGTCGGTG
CACAGGTGCGAACCTCCTGATGCTGTGGTGTGGCCCCAGAACGTGGAGCAGGTCAGCCGG
CTGGCAGCCCTGTGCTATCGCCAAGGTGTGCCCATCATCCCATTCGGCACCGGCACCGGG
CTTGAGGGTGGCGTCTGTGCTGTGCAGGGCGGCGTCTGCGTTAACCTGACGCATATGGAC
CGAATCCTGGAGCTGAACCAGGAGGACTTCTCTGTGGTGGTGGAGCCAGGTGTCACCCGC
AAAGCCCTCAACGCCCACCTGCGGGACAGCGGCCTCTGGTTTCCCGTGGACCCAGGCGCG
GACGCCTCTCTCTGTGGCATGGCGGCCACCGGGGCGTCGGGGACCAACGCGGTCCGCTAC
GGCACCATGCGGGACAACGTGCTCAACCTGGAGGTGGTGCTGCCCGACGGGCGGCTGCTG
CACACGGCGGGCCGAGGCCGGCATTTCCGCTTCGGCTTCTGGCCAGAAATCCCTCATCAC
ACAGCCTGGTACTCACCTTGTGTGTCCCTGGGACGTAGGAAGAGTGCAGCCGGCTACAAC
CTCACGGGGCTCTTCGTGGGCTCCGAGGGGACGCTGGGCCTCATCACAGCCACCACCCTG
CGCCTGCACCCTGCCCCTGAGGCCACAGTGGCCGCCACGTGTGCGTTCCCCAGTGTCCAG
GCTGCTGTGGACAGCACTGTACACATCCTCCAGGCTGCAGTGCCCGTAGCCCGCATTGAG
TTCCTGGATGAAGTCATGATGGATGCCTGCAACAGGTACAGCAAGCTGAATTGCTTAGTG
GCGCCCACACTCTTCCTGGAGTTCCATGGCTCCCAGCAGGCACTGGAGGAGCAGCTGCAG
CGCACAGAGGAGATAGTCCAGCAGAACGGAGCCTCTGACTTCTCCTGGGCCAAGGAGGCC
GAGGAGCGCAGCCGGCTTTGGACAGCACGGCACAATGCCTGGTACGCAGCCCTGGCCACG
CGGCCAGGCTGCAAGGGCTACTCCACGGATGTGTGTGTGCCCATCTCCCGGCTGCCGGAG
ATCGTGGTGCAGACCAAGGAGGATCTGAATGCCTCAGGACTCACAGGAAGCATTGTCGGG
CATGTGGGTGACGGCAACTTCCACTGCATCCTGCTGGTCAACCCTGATGACGCCGAGGAA
CTGGGCAGGGTCAAGGCTTTTGCAGAACAGCTGGGCAGGCGGGCACTGGCTCTCCACGGA
ACGTGCACGGGGGAGCATGGCATCGGAATGGGCAAGCGGCAGCTGCTGCAGGAGGAGGTG
GGCGCCGTGGGCGTGGAGACCATGCGGCAGCTCAAGGCCGTGCTAGACCCCCAAGGCCTC
ATGAATCCAGGCAAAGTGCTGTGA
Enzyme 2 GenBank Gene ID NM_153486.2 Link Image
Enzyme 2 GeneCard ID LDHD Link Image
Enzyme 2 GenAtlas ID LDHD Link Image
Enzyme 2 HGNC ID HGNC:19708 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 16q23.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Flick MJ, Konieczny SF: Identification of putative mammalian D-lactate dehydrogenase enzymes. Biochem Biophys Res Commun. 2002 Jul 26;295(4):910-6. [PubMed Link Image]
  2. 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 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 11578
Enzyme 3 Name Hydroxyacylglutathione hydrolase-like protein
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name HAGHL
Enzyme 3 Protein Sequence >Hydroxyacylglutathione hydrolase-like protein
MKVKVIPVLEDNYMYLVIEELTREAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHA
RGNPELARLRPGLAVLGADERIFSLTRRLAHGEELRFGAIHVRCLLTPGHTAGHMSYFLW
EDDCPDPPALFSGDALSVAGCGSCLEGSAQQMYQSLAELGTLPPETKVFCGHEHTLSNLE
FAQKVEPCNDHVRAKLSWAKARPLSRRGKRVGGEGTGFGVGGALRQGLMVTGACGHSRRG
MRMTCPLCRRLWARSASTTPSCGWREYGCCPGASTVTWTLRKASGDCVLG
Enzyme 3 Number of Residues 290
Enzyme 3 Molecular Weight 31557.1
Enzyme 3 Theoretical pI 8.27
Enzyme 3 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 3 General Function Involved in hydrolase activity
Enzyme 3 Specific Function Hydrolase acting on ester bonds (Potential)
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 46361987 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q6PII5 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name HAGHL_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >873 bp
ATGAAGGTCAAGGTCATCCCCGTGCTCGAGGACAACTACATGTACCTGGTCATCGAGGAG
CTCACGCGCGAGGCGGTGGCCGTGGACGTGGCTGTGCCCAAGAGGCTGCTGGAGATCGTG
GGCCGGGAGGGGGTGTCTCTGACCGCTGTGCTGACCACCCACCATCACTGGGACCACGCG
CGGGGAAACCCGGAGCTGGCGCGGCTTCGTCCCGGGCTGGCGGTGCTGGGCGCGGACGAG
CGCATCTTCTCGCTGACGCGCAGGCTGGCGCACGGCGAGGAGCTGCGGTTCGGGGCCATC
CACGTGCGTTGCCTCCTGACGCCCGGCCACACCGCCGGCCACATGAGCTACTTCCTGTGG
GAGGACGATTGCCCGGACCCACCCGCCCTGTTCTCGGGCGACGCGCTGTCGGTGGCCGGC
TGCGGCTCGTGCCTGGAGGGCAGCGCCCAGCAGATGTACCAGAGCCTGGCCGAGCTGGGT
ACCCTGCCCCCCGAGACGAAGGTGTTCTGCGGCCACGAGCACACGCTTAGCAACCTGGAG
TTTGCCCAGAAAGTGGAGCCCTGCAACGACCACGTGAGAGCCAAGCTGTCCTGGGCTAAG
GCACGGCCCCTTTCCCGCCGCGGCAAGAGGGTGGGGGGGGAGGGAACAGGCTTCGGGGTG
GGGGGGGCTCTCAGACAAGGCCTAATGGTGACCGGGGCCTGTGGTCACTCCAGAAGAGGG
ATGAGGATGACGTGCCCACTGTGCCGTCGACTCTGGGCGAGGAGCGCCTCTACAACCCCT
TCCTGCGGGTGGCGTGAGTATGGCTGTTGTCCCGGGGCCTCCACCGTTACGTGGACCCTT
AGGAAGGCATCTGGGGACTGCGTGTTGGGCTGA
Enzyme 3 GenBank Gene ID NM_207112.1 Link Image
Enzyme 3 GeneCard ID HAGHL Link Image
Enzyme 3 GenAtlas ID HAGHL Link Image
Enzyme 3 HGNC ID HGNC:14177 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 16p13.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. 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]
  2. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
  3. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [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]
Enzyme 3 Metabolite References Not Available