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Literature summary for 2.2.1.6 extracted from

  • Lonhienne, T.; Garcia, M.; Noble, C.; Harmer, J.; Fraser, J.; Williams, C.; Guddat, L.
    High resolution crystal structures of the acetohydroxyacid synthase-pyruvate complex provide new insights into its catalytic mechanism (2017), ChemistrySelect, 2, 11981-11988 .
No PubMed abstract available
Search for more literature for 2.2.1.6

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with pyruvate Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
additional information the enzyme contains a divalent metal ion as cofactor Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 pyruvate Saccharomyces cerevisiae
-
 2-acetolactate + CO2
-
 ?
pyruvate + 2-oxobutyrate Saccharomyces cerevisiae
-
 2-acetohydroxybutyrate + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P07342
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 pyruvate
-
 Saccharomyces cerevisiae 2-acetolactate + CO2
-
 ?
pyruvate + 2-oxobutyrate
-
 Saccharomyces cerevisiae 2-acetohydroxybutyrate + CO2
-
 ?

Subunits

Subunits Comment Organism
homodimer x-ray crystallography Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
acetohydroxyacid synthase
-
 Saccharomyces cerevisiae
AHAS
-
 Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Saccharomyces cerevisiae
O2 each subunit contains two molecules of oxygen (O2(I) and O2(II)) Saccharomyces cerevisiae
thiamine diphosphate
-
 Saccharomyces cerevisiae