| Version |
2.5 |
| Creation Date |
2005-11-16 15:48:42 |
| Update Date |
2009-05-05 20:58:28 |
| Accession Number |
HMDB01066 |
| Secondary Accession Numbers |
Not Available |
| Common Name |
S-Lactoylglutathione |
| Description |
S-Lactoylglutathione is a substrate of lactoylglutathione lyase [EC 4.4.1.5] in pyruvate metabolism (KEGG). Another enzyme, glyoxalase I, synthesizes this compound by converting methylglyoxal and reduced glutathione to S-lactoylglutathione. S-D-lactoylglutathione can be hydrolysed by thiolesterases to reduced glutathione and D-lactate but also converted to N-D-lactoylcysteinylglycine and N-D-lactoylcysteine by gamma-glutamyl transferase and dipeptidase (PMID: 8632674). S-lactoylglutathione has also been shown to modulate microtubule assembly (PMID: 690442). |
| Synonyms |
- (R)-S-lactoylglutathione
- S-lactoyl-glutathione
- D-lactoylglutathione
- n-(n-l-gamma-glutamyl-S-(2-hydroxy-1-oxopropyl)-l-cysteinyl)-glycine
- S-D-lactoylglutathione
- S-lactate glutathione
- S-lactateglutathione
- S-lactylglutathione
- S-D-lactoyl-glutathione
- S-[(2R)-2-hydroxypropanoyl]-gamma-L-glutamyl-L-cysteinylglycine
- delta-lactoylglutathione
- S-delta-lactoylglutathione
- S-delta-lactoyl-glutathione
|
| Chemical IUPAC Name |
(2S)-2-amino-4-[[(1R)-1-(carboxymethylcarbamoyl)-2-(2-hydroxypropanoylsulfanyl)ethyl]carbamoyl]butanoic acid |
| Chemical Formula |
C13H21N3O8S |
| Chemical Structure |
 |
| Chemical Taxonomy |
| Kingdom |
|
| Super Class |
- Amino acids and Amino Acid conjugates
|
| Class |
|
| Sub Class |
|
| Family |
|
| Species |
- secondary alcohol
- primary amine
- primary aliphatic amine (alkylamine)
- carboxylic acid
- secondary carboxylic acid amide
- thiocarboxylic acid ester
- alpha-aminoacid
|
| Biofunction |
- Component of Pyruvate metabolism
|
| Application |
| — |
| Source |
|
|
| Average Molecular Weight |
379.386 |
| Monoisotopic Molecular Weight |
379.104950 |
| Isomeric SMILES |
C[C@@H](O)C(=O)SC[C@H](NC(=O)CC[C@H](N)C(O)=O)C(=O)NCC(O)=O |
| Canonical SMILES |
CC(O)C(=O)SCC(NC(=O)CCC(N)C(O)=O)C(=O)NCC(O)=O |
| KEGG Compound ID |
C03451  |
| BioCyc ID |
S-LACTOYL-GLUTATHIONE  |
| BiGG ID |
41876  |
| Wikipedia Link |
Not Available |
| NuGOwiki Link |
HMDB01066  |
| Metagene Link |
HMDB01066  |
| METLIN ID |
5979  |
| PubChem Compound |
119450  |
| PubChem Substance |
8143378  |
| ChEBI ID |
15694  |
| CAS Registry Number |
25138-66-3 |
| InChI Identifier |
InChI=1/C13H21N3O8S/c1-6(17)13(24)25-5-8(11(21)15-4-10(19)20)16-9(18)3-2-7(14)12(22)23/h6-8,17H,2-5,14H2,1H3,(H,15,21)(H,16,18)(H,19,20)(H,22,23)/t6-,7+,8+/m1/s1 |
| Synthesis Reference |
Liu, Yan; Hama, Hideki; Fujita, Yasuya; Kondo, Akihiko; Inoue, Yoshiharu; Kimura, Akira; Fu Production of S-lactoylglutathione by high activity whole cell biocatalysts prepared by permeabilization of recombinant Saccharomyces cerevisiae with alcohols. |
| Melting Point (Experimental) |
Not Available |
| Experimental Water Solubility |
Not Available
Source: PhysProp
|
| Predicted Water Solubility |
7.55 mg/mL [Predicted by ALOGPS]
Calculated using ALOGPS
|
| Physiological Charge |
-1 |
| State |
Solid |
| Experimental LogP/Hydrophobicity |
Not Available
Source: PhysProp
|
| Predicted LogP/Hydrophobicity |
-2.88 [Predicted by ALOGPS]; -7.2 [Predicted by PubChem via XLOGP]
Calculated using ALOGPS
|
| Material Safety Data Sheet (MSDS) |
Not Available |
| MOL File |
Show |
| SDF File |
Show |
| PDB File |
Show |
| 2D Structure |
|
| 3D Structure |
|
| Experimental PDB ID |
Not Available |
| Experimental 1H NMR Spectrum |
Not Available |
| Experimental 13C NMR Spectrum |
Not Available |
| Experimental 13C HSQC Spectrum |
Not Available |
| Predicted 1H NMR Spectrum |
Show Image Show Peaklist
|
| Predicted 13C NMR Spectrum |
Show Image Show Peaklist
|
| Mass Spectrum |
Not Available |
| Simplified TOCSY Spectrum |
Not Available |
| BMRB Spectrum |
Not Available |
| Cellular Location |
- Cytoplasm (Predicted from LogP)
- mitochondria
|
| Biofluid Location |
Not Available |
| Tissue Location |
Not Available |
| Concentrations (Normal) |
Not Available |
| Concentrations (Abnormal) |
Not Available |
| Associated Disorders |
Not Available |
| OMIM ID |
Not Available |
| Pathways |
|
| General References |
- Edwards LG, Adesida A, Thornalley PJ: Inhibition of human leukaemia 60 cell growth by S-D-lactoylglutathione in vitro. Mediation by metabolism to N-D-lactoylcysteine and induction of apoptosis. Leuk Res. 1996 Jan;20(1):17-26. [PubMed
]
- Thornalley PJ: Advances in glyoxalase research. Glyoxalase expression in malignancy, anti-proliferative effects of methylglyoxal, glyoxalase I inhibitor diesters and S-D-lactoylglutathione, and methylglyoxal-modified protein binding and endocytosis by the advanced glycation endproduct receptor. Crit Rev Oncol Hematol. 1995 Aug;20(1-2):99-128. [PubMed
]
- Irsch T, Krauth-Siegel RL: Glyoxalase II of African trypanosomes is trypanothione-dependent. J Biol Chem. 2004 May 21;279(21):22209-17. Epub 2004 Feb 19. [PubMed
]
|
| Metabolic Enzymes |
- Lactoylglutathione lyase
- Hydroxyacylglutathione hydrolase
- Hydroxyacylglutathione hydrolase-like protein
|
|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5629 |
| Enzyme 1 Name |
Lactoylglutathione lyase |
| Enzyme 1 Synonyms |
- Methylglyoxalase
- Aldoketomutase
- Glyoxalase I
- Glx I
- Ketone-aldehyde mutase
- S-D- lactoylglutathione methylglyoxal lyase
|
| Enzyme 1 Gene Name |
GLO1 |
| Enzyme 1 Protein Sequence |
>Lactoylglutathione lyase
MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQK
CDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNS
DPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKM
ATLM
|
| Enzyme 1 Number of Residues |
184 |
| Enzyme 1 Molecular Weight |
20778 |
| Enzyme 1 Theoretical pI |
4.92 |
| Enzyme 1 GO Classification |
| Function |
- carbon-sulfur lyase activity
- catalytic activity
- lactoylglutathione lyase activity
- lyase activity
|
| Process |
- carbohydrate metabolism
- macromolecule metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Amino acid transport and metabolism |
| Enzyme 1 Specific Function |
Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- (R)-S-lactoylglutathione = glutathione + methylglyoxal
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
219664  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q04760  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
LGUL_HUMAN  |
| Enzyme 1 PDB ID |
1QIP  |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>555 bp
ATGGCAGAACCGCAGCCCCCGTCCGGCGGCCTCACGGACGAGGCCGCCCTCAGTTGCTGC
TCCGACGCGGACCCCAGTACCAAGGATTTTCTATTGCAGCAGACCATGCTACGAGTGAAG
GATCCTAAGAAGTCACTGGATTTTTATACTAGAGTTCTTGGAATGACGCTAATCCAAAAA
TGTGATTTTCCCATTATGAAGTTTTCACTCTACTTCTTGGCTTATGAGGATAAAAATGAC
ATCCCTAAAGAAAAAGATGAAAAAATAGCCTGGGCGCTCTCCAGAAAAGCTACACTTGAG
CTGACACACAATTGGGGCACTGAAGATGATGCGACCCAGAGTTACCACAATGGCAATTCA
GACCCTCGAGGATTCGGTCATATTGGAATTGCTGTTCCTGATGTATACAGTGCTTGTAAA
AGGTTTGAAGAACTGGGAGTCAAATTTGTGAAGAAACCTGATGATGGTAAAATGAAAGGC
CTGGCATTTATTCAAGATCCTGATGGCTACTGGATTGAAATTTTGAATCCTAACAAAATG
GCAACCTTAATGTAG
|
| Enzyme 1 GenBank Gene ID |
D13315  |
| Enzyme 1 GeneCard ID |
GLO1  |
| Enzyme 1 GenAtlas ID |
GLO1  |
| Enzyme 1 HGNC ID |
HGNC:4323  |
| Enzyme 1 Chromosome Location |
6 |
| Enzyme 1 Locus |
6p21.3-p21.1 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Kim NS, Umezawa Y, Ohmura S, Kato S: Human glyoxalase I. cDNA cloning, expression, and sequence similarity to glyoxalase I from Pseudomonas putida. J Biol Chem. 1993 May 25;268(15):11217-21. [PubMed
]
- Ranganathan S, Walsh ES, Godwin AK, Tew KD: Cloning and characterization of human colon glyoxalase-I. J Biol Chem. 1993 Mar 15;268(8):5661-7. [PubMed
]
- Ridderstrom M, Mannervik B: Optimized heterologous expression of the human zinc enzyme glyoxalase I. Biochem J. 1996 Mar 1;314 ( Pt 2):463-7. [PubMed
]
- Ranganathan S, Ciaccio PJ, Walsh ES, Tew KD: Genomic sequence of human glyoxalase-I: analysis of promoter activity and its regulation. Gene. 1999 Nov 15;240(1):149-55. [PubMed
]
- 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
]
- Cameron AD, Olin B, Ridderstrom M, Mannervik B, Jones TA: Crystal structure of human glyoxalase I--evidence for gene duplication and 3D domain swapping. EMBO J. 1997 Jun 16;16(12):3386-95. [PubMed
]
- Ridderstrom M, Cameron AD, Jones TA, Mannervik B: Involvement of an active-site Zn2+ ligand in the catalytic mechanism of human glyoxalase I. J Biol Chem. 1998 Aug 21;273(34):21623-8. [PubMed
]
- Cameron AD, Ridderstrom M, Olin B, Kavarana MJ, Creighton DJ, Mannervik B: Reaction mechanism of glyoxalase I explored by an X-ray crystallographic analysis of the human enzyme in complex with a transition state analogue. Biochemistry. 1999 Oct 12;38(41):13480-90. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
6092 |
| Enzyme 2 Name |
Hydroxyacylglutathione hydrolase |
| Enzyme 2 Synonyms |
- Glyoxalase II
- GLX II
|
| Enzyme 2 Gene Name |
HAGH |
| Enzyme 2 Protein Sequence |
>Hydroxyacylglutathione hydrolase
MKVEVLPALTDNYMYLVIDDETKEAAIVDPVQPQKVVDAARKHGVKLTTVLTTHHHWDHA
GGNEKLVKLESGLKVYGGDDRIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVS
KPGGSEPPAVFTGDTLFVAGCGKFYEGTADEMCKALLEVLGRLPPDTRVYCGHEYTINNL
KFARHVEPGNAAIREKLAWAKEKYSIGEPTVPSTLAEEFTYNPFMRVREKTVQQHAGETD
PVTTMRAVRREKDQFKMPRD
|
| Enzyme 2 Number of Residues |
260 |
| Enzyme 2 Molecular Weight |
28860 |
| Enzyme 2 Theoretical pI |
7.36 |
| Enzyme 2 GO Classification |
Not Available |
| Enzyme 2 General Function |
Not Available |
| Enzyme 2 Specific Function |
Thiolesterase that catalyzes the hydrolysis of S-D- lactoyl-glutathione to form glutathione and D-lactic acid |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
1237213  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q16775  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
GLO2_HUMAN  |
| Enzyme 2 PDB ID |
1QH3  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>783 bp
ATGAAGGTAGAGGTGCTGCCTGCCCTGACCGACAACTACATGTACCTGGTCATTGATGAT
GAGACCAAGGAGGCTGCCATTGTGGATCCGGTGCAGCCCCAGAAGGTCGTGGACGCGGCG
AGAAAGCACGGGGTGAAACTGACCACAGTGCTCACCACCCACCACCACTGGGACCATGCT
GGCGGGAATGAGAAACTGGTCAAGCTGGAGTCGGGACTGAAGGTGTACGGGGGTGACGAC
CGTATCGGGGCCCTGACTCACAAGATCACTCACCTGTCCACACTGCAGGTGGGGTCTCTG
AACGTCAAGTGCCTGGCGACCCCGTGCCACACTTCAGGACACATTTGTTACTTCGTGAGC
AAGCCCGGAGGCTCGGAGCCCCCTGCCGTGTTCACAGGTGACACCTTGTTTGTGGCTGGC
TGCGGGAAGTTCTATGAAGGGACTGCGGATGAGATGTGTAAAGCTCTGCTGGAGGTCTTG
GGCCGGCTCCCCCCGGACACAAGAGTCTACTGTGGCCACGAGTACACCATCAACAACCTC
AAGTTTGCACGCCACGTGGAGCCCGGCAATGCCGCCATCCGGGAGAAGCTGGCCTGGGCC
AAGGAGAAGTACAGCATCGGGGAGCCCACAGTGCCATCCACCCTGGCAGAGGAGTTTACC
TACAACCCCTTCATGAGAGTGAGGGAGAAGACGGTGCAGCAGCACGCAGGTGAGACGGAC
CCGGTGACCACCATGCGGGCCGTGCGCAGGGAGAAGGACCAGTTCAAGATGCCCCGGGAC
TGA
|
| Enzyme 2 GenBank Gene ID |
X90999  |
| Enzyme 2 GeneCard ID |
HAGH  |
| Enzyme 2 GenAtlas ID |
HAGH  |
| Enzyme 2 HGNC ID |
HGNC:4805  |
| Enzyme 2 Chromosome Location |
16 |
| Enzyme 2 Locus |
16p13.3 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- 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
]
- 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
]
- 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
]
|
| 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 |
31558 |
| Enzyme 3 Theoretical pI |
Not Available |
| Enzyme 3 GO Classification |
Not Available |
| Enzyme 3 General Function |
Not Available |
| Enzyme 3 Specific Function |
Not Available |
| Enzyme 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
- H2O + (R)-S-Lactoylglutathione --> Reduced glutathione + H+ + D-Lactate
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
45708670  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q6PII5  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
Q6PII5_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
Not Available |
| Enzyme 3 GenBank Gene ID |
BC033796  |
| Enzyme 3 GeneCard ID |
Not Available |
| Enzyme 3 GenAtlas ID |
HAGHL  |
| Enzyme 3 HGNC ID |
HGNC:14177  |
| Enzyme 3 Chromosome Location |
Not Available |
| Enzyme 3 Locus |
Not Available |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |