Enzyme

Download
EC Tree
     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.1 Hydro-lyases
ID:4.2.1.169
Description:3-vinylbacteriochlorophyllide d 3(1)-hydratase.

3D structure

Click one PDB to see exact 3D structure provided by NGL.

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.

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.1.169
BRENDA Enzyme Link: BRENDA 4.2.1.169
KEGG Enzyme Link: KEGG4.2.1.169
BioCyc Enzyme Link: BioCyc 4.2.1.169
ExPASy Enzyme Link: ExPASy4.2.1.169
EC2PDB Enzyme Link: EC2PDB 4.2.1.169
ExplorEnz Enzyme Link: ExplorEnz 4.2.1.169
PRIAM enzyme-specific profiles Link: PRIAM 4.2.1.169
IntEnz Enzyme Link: IntEnz 4.2.1.169
MEDLINE Enzyme Link: MEDLINE 4.2.1.169
MSA:

4.2.1.169;

Phylogenetic Tree:

4.2.1.169;

Uniprot:
M-CSA:
RHEA:49188 a bacteriochlorophyllide d = a 3-vinylbacteriochlorophyllide d + H2O
RULE(radius=1) [*:1]-[CH;+0:2](-[CH3;+0:3])-[OH;+0:4]>>[*:1]-[CH;+0:2]=[CH2;+0:3].[OH2;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Stereochemical conversion of C3-vinyl group to 1-hydroxyethyl group in bacteriochlorophyll c by the hydratases BchF and BchV: adaptation of green sulfur bacteria to limited-light environments.Harada J, Teramura M, Mizoguchi T, Tsukatani Y, Yamamoto K, Tamiaki H2015 Dec26331578
Chlorobium tepidum: insights into the structure, physiology, and metabolism of a green sulfur bacterium derived from the complete genome sequence.Frigaard NU, Chew AG, Li H, Maresca JA, Bryant DA200316245042