KEGG   ENZYME: 1.1.1.110Help
Entry
EC 1.1.1.110                Enzyme                                 

Name
aromatic 2-oxoacid reductase;
(R)-aromatic lactate dehydrogenase;
(R)-4-hydroxyphenyllactate dehydrogenase;
indolelactate:NAD+ oxidoreductase;
indolelactate dehydrogenase;
fldH (gene name);
(indol-3-yl)lactate:NAD+ oxidoreductase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
aromatic 2-oxoacid:NAD+ oxidoreductase
Reaction(IUBMB)
(1) (R)-3-(phenyl)lactate + NAD+ = 3-phenylpyruvate + NADH + H+ [RN:R01370];
(2) (R)-3-(4-hydroxyphenyl)lactate + NAD+ = 3-(4-hydroxyphenyl)pyruvate + NADH + H+ [RN:R03337];
(3) (R)-(indol-3-yl)lactate + NAD+ = (indol-3-yl)pyruvate + NADH + H+ [RN:R12256]
Reaction(KEGG)
Substrate
(R)-3-(phenyl)lactate [CPD:C05607];
NAD+ [CPD:C00003];
(R)-3-(4-hydroxyphenyl)lactate [CPD:C03964];
(R)-(indol-3-yl)lactate [CPD:C22006]
Product
3-phenylpyruvate;
NADH [CPD:C00004];
H+ [CPD:C00080];
3-(4-hydroxyphenyl)pyruvate [CPD:C01179];
(indol-3-yl)pyruvate [CPD:C00331]
Comment
The enzymes from anaerobic bacteria such as Clostridium sporogenes participate in the fermentation pathways of L-phenylalanine, L-tyrosine and L-tryptophan. The enzyme from the yeast Candida maltosa has similar activity, but, unlike the bacterial enzyme, requires Mn2+ and can also use NADPH with lower activity.
History
EC 1.1.1.110 created 1972 (EC 1.1.1.222 created 2000, incorporated 2018), modified 2018
Pathway
ec00380  Tryptophan metabolism
Reference
1  [PMID:4384683]
  Authors
Jean M, DeMoss RD.
  Title
Indolelactate dehydrogenase from Clostridium sporogenes.
  Journal
Can J Microbiol 14:429-35 (1968)
Reference
2  [PMID:6354130]
  Authors
Giesel H, Simon H
  Title
On the occurrence of enoate reductase and 2-oxo-carboxylate reductase in clostridia and some observations on the amino acid fermentation by Peptostreptococcus anaerobius.
  Journal
Arch Microbiol 135:51-7 (1983)
Reference
3
  Authors
Bode, R., Lippoldt, A. and Birnbaum, D.
  Title
Purification and properties of D-aromatic lactate dehydrogenase an enzyme involved in the catabolism of the aromatic amino acids of Candida maltosa.
  Journal
Biochem Physiol Pflanzen 181:189-198 (1986)
Reference
4  [PMID:10849007]
  Authors
Dickert S, Pierik AJ, Linder D, Buckel W.
  Title
The involvement of coenzyme A esters in the dehydration of (R)-phenyllactate to (E)-cinnamate by Clostridium sporogenes.
  Journal
Eur J Biochem 267:3874-84 (2000)
DOI:10.1046/j.1432-1327.2000.01427.x
  Sequence
Reference
5  [PMID:29168502]
  Authors
Dodd D, Spitzer MH, Van Treuren W, Merrill BD, Hryckowian AJ, Higginbottom SK, Le A, Cowan TM, Nolan GP, Fischbach MA, Sonnenburg JL
  Title
A gut bacterial pathway metabolizes aromatic amino acids into nine circulating metabolites.
  Journal
Nature 551:648-652 (2017)
DOI:10.1038/nature24661
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.110
IUBMB Enzyme Nomenclature: 1.1.1.110
ExPASy - ENZYME nomenclature database: 1.1.1.110
BRENDA, the Enzyme Database: 1.1.1.110
CAS: 37250-41-2

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