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Literature summary for 4.2.1.112 extracted from

  • Yadav, J.; Das, S.K.; Sarkar, S.
    A functional mimic of the new class of tungstoenzyme acetylene hydratase (1997), J. Am. Chem. Soc., 119, 4315-4316.
No PubMed abstract available
Search for more literature for 4.2.1.112

Metals/Ions

Metals/Ions Comment Organism Structure
Iron the enzyme is a tungsten/iron-sulfur protein Syntrophotalea acetylenica
Molybdenum molybdopterin-guanine dinucleotide cofactor Syntrophotalea acetylenica
Tungsten dependent on, tungstoenzyme Syntrophotalea acetylenica

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
73000
-
 1 * 73000 Syntrophotalea acetylenica

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetylene + H2O Syntrophotalea acetylenica
-
 acetaldehyde
-
 r

Organism

Organism UniProt Comment Textmining
Syntrophotalea acetylenica
-
-
-

Reaction

Reaction Comment Organism Reaction ID
acetaldehyde = acetylene + H2O reaction mechanism involving molybdenum-cofactor and tungsten/iron-sulfur cluster, structure-function modeling, overview Syntrophotalea acetylenica
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetylene + H2O
-
 Syntrophotalea acetylenica acetaldehyde
-
 r
acetylene + H2O the hydration reaction is unique for a tungsten and molybdenum containing enzyme, which are usually redox enzymes Syntrophotalea acetylenica acetaldehyde
-
 r

Subunits

Subunits Comment Organism
monomer 1 * 73000 Syntrophotalea acetylenica

Synonyms

Synonyms Comment Organism
AH
-
 Syntrophotalea acetylenica

Cofactor

Cofactor Comment Organism Structure
molybdopterin guanine dinucleotide structure-function analysis Syntrophotalea acetylenica