EC number:3.5.4.27

Enzyme

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     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.4 In cyclic amidines
ID:3.5.4.27
Description:Methenyltetrahydromethanopterin cyclohydrolase.
Alternative Name: Methenyl-H(4)MPT cyclohydrolase.
Cath: 3.30.1030.10; 3.10.340.11;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.4.27
BRENDA Enzyme Link: BRENDA 3.5.4.27
KEGG Enzyme Link: KEGG3.5.4.27
BioCyc Enzyme Link: BioCyc 3.5.4.27
ExPASy Enzyme Link: ExPASy3.5.4.27
EC2PDB Enzyme Link: EC2PDB 3.5.4.27
ExplorEnz Enzyme Link: ExplorEnz 3.5.4.27
PRIAM enzyme-specific profiles Link: PRIAM 3.5.4.27
IntEnz Enzyme Link: IntEnz 3.5.4.27
MEDLINE Enzyme Link: MEDLINE 3.5.4.27

EC number:3.5.4.27

MSA:

3.5.4.27;
Phylogenetic Tree:

3.5.4.27;
Uniprot:
M-CSA:
RHEA:19053 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = H(+) + N(5)-formyl-5,6,7,8-tetrahydromethanopterin
RULE(radius=1) [*:1]-[N;H0;+0:2]1-[*:3]-[*:4]-[N+;H0:5](-[*:6])=[CH;+0:7]-1.[OH2;+0:8]>>[*:1]-[NH;+0:2]-[*:3]-[*:4]-[N;H0;+0:5](-[*:6])-[CH;+0:7]=[O;H0;+0:8]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Methenyl-tetrahydromethanopterin cyclohydrolase in cell extracts of Methanobacterium.Donnelly MI, Escalante-Semerena JC, Rinehart KL Jr, Wolfe RS1985 Nov 14062290
Structure and catalytic mechanism of N(5),N(10)-methenyl-tetrahydromethanopterin cyclohydrolase.Upadhyay V, Demmer U, Warkentin E, Moll J, Shima S, Ermler U2012 Oct 2323013430
The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from the hyperthermophilic archaeon Methanopyrus kandleri.Grabarse W, Vaupel M, Vorholt JA, Shima S, Thauer RK, Wittershagen A, Bourenkov G, Bartunik HD, Ermler U1999 Oct 1510545331