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
ec00350  Tyrosine metabolism
ec00360  Phenylalanine metabolism
ec00380  Tryptophan metabolism
ec00960  Tropane, piperidine and pyridine alkaloid biosynthesis
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K23109  aromatic 2-oxoacid reductase
Genes
CBO: CBO3284(fldH)
CBA: CLB_3340(ldhA-2)
CBH: CLC_3226(ldhA-2)
CBY: CLM_3717(ldhA)
CBL: CLK_2700
CBB: CLD_1239
CBI: CLJ_B3564
CBF: CLI_3454(ldhA-2)
CBM: CBF_3436(ldhA-2)
CBJ: H04402_03369
CLD: CLSPO_c34040(fldH)
 » show all
Taxonomy
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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