EC number:4.2.1.112

Enzyme

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     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.1 Hydro-lyases
ID:4.2.1.112
Description:Acetylene hydratase.
Alternative Name: AHy.
Cath: 3.40.50.740; 2.20.25.90; 2.40.40.20; 3.40.228.10;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.1.112
BRENDA Enzyme Link: BRENDA 4.2.1.112
KEGG Enzyme Link: KEGG4.2.1.112
BioCyc Enzyme Link: BioCyc 4.2.1.112
ExPASy Enzyme Link: ExPASy4.2.1.112
EC2PDB Enzyme Link: EC2PDB 4.2.1.112
ExplorEnz Enzyme Link: ExplorEnz 4.2.1.112
PRIAM enzyme-specific profiles Link: PRIAM 4.2.1.112
IntEnz Enzyme Link: IntEnz 4.2.1.112
MEDLINE Enzyme Link: MEDLINE 4.2.1.112

EC number:4.2.1.112

MSA:

4.2.1.112;
Phylogenetic Tree:

4.2.1.112;
Uniprot:
M-CSA:
RHEA:17885 acetaldehyde = acetylene + H2O
RULE(radius=1) [CH3;+0:1]-[CH;+0:2]=[O;H0;+0:3]>>[CH;+0:2]#[CH;+0:1].[OH2;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Purification and characterization of acetylene hydratase of Pelobacter acetylenicus, a tungsten iron-sulfur protein.Rosner BM, Schink B1995 Oct7592321
Exploring the active site of the tungsten, iron-sulfur enzyme acetylene hydratase.Tenbrink F, Schink B, Kroneck PM2011 Mar21193613
Mechanism of tungsten-dependent acetylene hydratase from quantum chemical calculations.Liao RZ, Yu JG, Himo F2010 Dec 2821149684
Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase.Seiffert GB, Ullmann GM, Messerschmidt A, Schink B, Kroneck PM, Einsle O2007 Feb 2717360611