ID: | 3.1.2.28 |
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Description: | 1,4-dihydroxy-2-naphthoyl-CoA hydrolase. |
Cath: | 1.10.12.10; 1.10.12.100; 3.90.226.10; 3.10.129.10; |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 3.1.2.28 |
BRENDA Enzyme Link: | BRENDA 3.1.2.28 |
KEGG Enzyme Link: | KEGG3.1.2.28 |
BioCyc Enzyme Link: | BioCyc 3.1.2.28 |
ExPASy Enzyme Link: | ExPASy3.1.2.28 |
EC2PDB Enzyme Link: | EC2PDB 3.1.2.28 |
ExplorEnz Enzyme Link: | ExplorEnz 3.1.2.28 |
PRIAM enzyme-specific profiles Link: | PRIAM 3.1.2.28 |
IntEnz Enzyme Link: | IntEnz 3.1.2.28 |
MEDLINE Enzyme Link: | MEDLINE 3.1.2.28 |
RHEA:26309 | 1,4-dihydroxy-2-naphthoyl-CoA + H2O = 1,4-dihydroxy-2-naphthoate + CoA + H(+) |
RULE(radius=1) | [*:1]=[C;H0;+0:2](-[*:3])-[S;H0;+0:4]-[*:5].[OH2;+0:6]>>[*:5]-[SH;+0:4].[*:1]=[C;H0;+0:2](-[*:3])-[OH;+0:6] |
Reaction | ![]() |
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Core-to-Core |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Phylloquinone (vitamin K(1) ) biosynthesis in plants: two peroxisomal thioesterases of Lactobacillales origin hydrolyze 1,4-dihydroxy-2-naphthoyl-CoA. | Widhalm JR, Ducluzeau AL, Buller NE, Elowsky CG, Olsen LJ, Basset GJ | 2012 Jul | 22372525 |
A dedicated thioesterase of the Hotdog-fold family is required for the biosynthesis of the naphthoquinone ring of vitamin K1. | Widhalm JR, van Oostende C, Furt F, Basset GJ | 2009 Apr 7 | 19321747 |