EC number:1.4.1.20

Enzyme

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     1. Oxidoreductases
        1.4 Acting on the CH-NH2 group of donors
            1.4.1 With NAD+ or NADP+ as acceptor
ID:1.4.1.20
Description:Phenylalanine dehydrogenase.
Alternative Name: PheDH.
L-phenylalanine dehydrogenase.
Prosite: PDOC00071;
PDB:
PDBScop
Cath: 3.40.50.720; 3.40.50.10860;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.4.1.20
BRENDA Enzyme Link: BRENDA 1.4.1.20
KEGG Enzyme Link: KEGG1.4.1.20
BioCyc Enzyme Link: BioCyc 1.4.1.20
ExPASy Enzyme Link: ExPASy1.4.1.20
EC2PDB Enzyme Link: EC2PDB 1.4.1.20
ExplorEnz Enzyme Link: ExplorEnz 1.4.1.20
PRIAM enzyme-specific profiles Link: PRIAM 1.4.1.20
IntEnz Enzyme Link: IntEnz 1.4.1.20
MEDLINE Enzyme Link: MEDLINE 1.4.1.20

EC number:1.4.1.20

MSA:

1.4.1.20;
Phylogenetic Tree:

1.4.1.20;
Uniprot:
M-CSA:
RHEA:21408 H2O + L-phenylalanine + NAD(+) = 3-phenylpyruvate + H(+) + NADH + NH4(+)
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[NH2;+0:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1.[OH2;+0:13]>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:13].[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1.[NH3;+0:4]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Rhodococcus L-phenylalanine dehydrogenase: kinetics, mechanism, and structural basis for catalytic specificity.Brunhuber NM, Thoden JB, Blanchard JS, Vanhooke JL2000 Aug 810924111
Phenylalanine dehydrogenase from Rhodococcus sp. M4: high-resolution X-ray analyses of inhibitory ternary complexes reveal key features in the oxidative deamination mechanism.Vanhooke JL, Thoden JB, Brunhuber NM, Blanchard JS, Holden HM1999 Feb 2310029526