KEGG   ENZYME: 4.2.1.112
Entry
EC 4.2.1.112                Enzyme                                 
Name
acetylene hydratase;
AH;
acetaldehyde hydro-lyase
Class
Lyases;
Carbon-oxygen lyases;
Hydro-lyases
Sysname
acetaldehyde hydro-lyase (acetylene-forming)
Reaction(IUBMB)
acetaldehyde = acetylene + H2O [RN:R05380]
Reaction(KEGG)
R05380
Substrate
acetaldehyde [CPD:C00084]
Product
acetylene [CPD:C01548];
H2O [CPD:C00001]
Comment
This is a non-redox-active enzyme that contains two molybdopterin guanine dinucleotide (MGD) cofactors, a tungsten centre and a cubane type [4Fe-4S] cluster [2].The tungsten centre binds a water molecule that is activated by an adjacent aspartate residue, enabling it to attack acetylene bound in a distinct hydrophobic pocket [2]. Ethylene cannot act as a substrate [1].
History
EC 4.2.1.112 created 2007
Pathway
ec00625  Chloroalkane and chloroalkene degradation
ec01120  Microbial metabolism in diverse environments
Orthology
K20625  acetylene hydratase
Genes
MRPNM686_006105
FCEJN531_006555
PECTBN1012_Phect1753
SNEANBZ79_05880
PACEA6070_04635
PEFA7E78_00110
RTSCE91St31_08480
DHILH044_17625
Reference
1  [PMID:7592321]
  Authors
Rosner BM, Schink B
  Title
Purification and characterization of acetylene hydratase of Pelobacter acetylenicus, a tungsten iron-sulfur protein.
  Journal
J Bacteriol 177:5767-72 (1995)
DOI:10.1128/JB.177.20.5767-5772.1995
  Sequence
Reference
2  [PMID:17360611]
  Authors
Seiffert GB, Ullmann GM, Messerschmidt A, Schink B, Kroneck PM, Einsle O
  Title
Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase.
  Journal
Proc Natl Acad Sci U S A 104:3073-7 (2007)
DOI:10.1073/pnas.0610407104
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 4.2.1.112
IUBMB Enzyme Nomenclature: 4.2.1.112
ExPASy - ENZYME nomenclature database: 4.2.1.112
UM-BBD (Biocatalysis/Biodegradation Database): 4.2.1.112
BRENDA, the Enzyme Database: 4.2.1.112
CAS: 75788-81-7
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