Indolelactate dehydrogenase

From Wikipedia, the free encyclopedia

In enzymology, an indolelactate dehydrogenase (EC 1.1.1.110) is an enzyme that catalyzes the chemical reaction

(indol-3-yl)lactate + NAD⁺ (indol-3-yl)pyruvate + NADH + H⁺

Thus, the two substrates of this enzyme are (indol-3-yl)lactate and NAD⁺, whereas its 3 products are (indol-3-yl)pyruvate, NADH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (indol-3-yl)lactate:NAD+ oxidoreductase. This enzyme is also called indolelactate:NAD+ oxidoreductase. This enzyme participates in tryptophan metabolism.

[edit] References

• IUBMB entry for 1.1.1.110
• BRENDA references for 1.1.1.110 (Recommended.)
• PubMed references for 1.1.1.110
• PubMed Central references for 1.1.1.110
• Google Scholar references for 1.1.1.110
• Jean M, DeMoss RD (1968). "Indolelactate dehydrogenase from Clostridium sporogenes". Can. J. Microbiol. 14: 429–35. PMID 4384683. 

[edit] External links

The CAS registry number for this enzyme class is 37250-41-2.

• IUBMB entry for 1.1.1.110

• KEGG entry for 1.1.1.110

• BRENDA entry for 1.1.1.110

• NiceZyme view of 1.1.1.110

• EC2PDB: PDB structures for 1.1.1.110

• PRIAM entry for 1.1.1.110

• PUMA2 entry for 1.1.1.110

• IntEnz: Integrated Enzyme entry for 1.1.1.110

• MetaCyc entry for 1.1.1.110

• Atomic-resolution structures of enzymes belonging to this class

[edit] Gene Ontology (GO) codes

• EGO entry for GO code 0047722: indolelactate dehydrogenase

• AMIGO entry for GO code 0047722: indolelactate dehydrogenase