KEGG ENZYME: 1.1.1.110

ENZYME: 1.1.1.110

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

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)

R01370 R03337 R12256

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

MSUT:

LC048_24585

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)

CCAA:

KQH81_13535

NBJ:	HXK95_000970

» show all

Reference

1 [PMID:4384683]

Authors

Jean M, DeMoss RD.

Title

Indolelactate dehydrogenase from Clostridium sporogenes.

Journal

Can J Microbiol 14:429-35 (1968)
DOI:10.1139/m68-068

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)
DOI:10.1007/bf00419482

Reference

Authors

Bode R, Lippoldt A, 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

[cld:CLSPO_c34040]

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

[cld:CLSPO_c34040]

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

LinkDB

DBGET integrated database retrieval system