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Literature summary for 2.3.1.30 extracted from

  • Johnson, C.M.; Roderick, S.L.; Cook, P.F.
    The serine acetyltransferase reaction: acetyl transfer from an acylpantothenyl donor to an alcohol (2005), Arch. Biochem. Biophys., 433, 85-95.
    View publication on PubMed
Search for more literature for 2.3.1.30

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray crystallographic structure of the enzyme in binary complexes with cysteine and CoA and refined to resolutions of 1.85 and 2.0 A, respectively Haemophilus influenzae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + L-serine Haemophilus influenzae enzyme catalyzes the committed step in the de novo synthesis of L-cysteine. Serine acetyltransferase is regulated by feedback inhibition by the end product L-cysteine, which acts by binding to the serine site in the active site and inducing a conformational change that prevents reactant binding CoA + O-acetyl-L-serine
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Organism

Organism UniProt Comment Textmining
Haemophilus influenzae
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Reaction

Reaction Comment Organism Reaction ID
acetyl-CoA + L-serine = CoA + O-acetyl-L-serine ordered kinetic mechanism with acetyl CoA bound prior to L-serine and O-acetyl-L-serine released prior to CoA. The rate-limiting step along the reaction pathway is the nucleophilic attack of the serine hydroxyl on the thioester of acetyl CoA. Product release contributes to rate-limitation at saturating concentrations of reactants. The reaction is catalyzed by an active site general base with a pK of 7, which accepts a proton from the serine hydroxyl as a tetrahedral intermediate is formed between the reactants, and donates it to the thiol of CoA as the intermediate collapses to give products Haemophilus influenzae
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + L-serine enzyme catalyzes the committed step in the de novo synthesis of L-cysteine. Serine acetyltransferase is regulated by feedback inhibition by the end product L-cysteine, which acts by binding to the serine site in the active site and inducing a conformational change that prevents reactant binding Haemophilus influenzae CoA + O-acetyl-L-serine
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 ?

Synonyms

Synonyms Comment Organism
HISAT
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 Haemophilus influenzae