EC |
1.2.1.101 |
Accepted name: |
L-tyrosine reductase |
Reaction: |
L-tyrosinal + NADP+ + AMP + diphosphate = L-tyrosine + NADPH + H+ + ATP |
Glossary: |
L-tyrosinal = (2S)-2-amino-3-(4-hydroxyphenyl)propanal |
Other name(s): |
lnaA (gene name); lnbA (gene name) |
Systematic name: |
(2S)-2-amino-3-(4-hydroxyphenyl)propanal:NADP+ oxidoreductase (ATP-forming) |
Comments: |
The enzyme, characterized from the ascomycete fungus Aspergillus flavus, is specific for L-tyrosine. It contains three domains - an adenylation domain, a peptidyl-carrier protein (PCP) domain, and a reductase domain, and requires activation by attachment of a phosphopantetheinyl group. The enzyme activates its substrate to an adenylate form, followed by a transfer to the PCP domain. The resulting thioester is subsequently transferred to the reductase domain, where it is reduced to the aldehyde. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9074-94-6 |
References: |
1. |
Forseth, R.R., Amaike, S., Schwenk, D., Affeldt, K.J., Hoffmeister, D., Schroeder, F.C. and Keller, N.P. Homologous NRPS-like gene clusters mediate redundant small-molecule biosynthesis in Aspergillus flavus. Angew. Chem. Int. Ed. Engl. 52 (2013) 1590–1594. [PMID: 23281040] |
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[EC 1.2.1.101 created 2018] |
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