Enzyme

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     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.1 Hydro-lyases
ID:4.2.1.51
Description:Prephenate dehydratase.
Prosite: PDOC00671;
PDB:
PDBScop
1ZNZ 8089792; 8089793;
1ZNY 8089792; 8089793;
1ZNX 8089792; 8089793;
1ZNW 8089792; 8089793;
1Z8F 8089792; 8089793;
 » show all

Cath: 1.20.5.1820; 3.30.70.260; 1.20.59.10; 3.40.190.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.1.51
BRENDA Enzyme Link: BRENDA 4.2.1.51
KEGG Enzyme Link: KEGG4.2.1.51
BioCyc Enzyme Link: BioCyc 4.2.1.51
ExPASy Enzyme Link: ExPASy4.2.1.51
EC2PDB Enzyme Link: EC2PDB 4.2.1.51
ExplorEnz Enzyme Link: ExplorEnz 4.2.1.51
PRIAM enzyme-specific profiles Link: PRIAM 4.2.1.51
IntEnz Enzyme Link: IntEnz 4.2.1.51
MEDLINE Enzyme Link: MEDLINE 4.2.1.51
MSA:

4.2.1.51;

Phylogenetic Tree:

4.2.1.51;

Uniprot:
M-CSA:
RHEA:21648 H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
RULE(radius=1) [*:1]=[C;H0;+0:2](-[OH;+0:3])-[C;H0;+0:4]1(-[*:5])-[CH;+0:6]=[CH;+0:7]-[CH;+0:8](-[OH;+0:9])-[CH;+0:10]=[CH;+0:11]-1.[H+;H0:12]>>[*:5]-[c;H0;+0:4]1:[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:[cH;+0:10]:[cH;+0:11]:1.[*:1]=[C;H0;+0:2]=[O;H0;+0:3].[OH2;+0:9]
Reaction
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References

TitleAuthorsDatePubMed ID
THE BIOSYNTHESIS OF PHENYLALANINE AND TYROSINE; ENZYMES CONVERTING CHORISMIC ACID INTO PREPHENIC ACID AND THEIR RELATIONSHIPS TO PREPHENATE DEHYDRATASE AND PREPHENATE DEHYDROGENASE.COTTON RG, GIBSON F1965 Apr 1214323651
pheA (Rv3838c) of Mycobacterium tuberculosis encodes an allosterically regulated monofunctional prephenate dehydratase that requires both catalytic and regulatory domains for optimum activity.Prakash P, Pathak N, Hasnain SE2005 May 2715753077
ENZYMATIC FORMATION OF PHENYLPYRUVIC ACID IN PSEUDOMONAS SP. (ATCC 11299A) AND ITS REGULATION.CERUTTI P, GUROFF G1965 Jul14342329