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Literature summary for 6.2.1.5 extracted from

  • Majumdar, R.; Guest, J.R.; Bridger, W.A.
    Functional consequences of substitution of the active site (phospho)histidine residue of Escherichia coli succinyl-CoA synthetase (1991), Biochim. Biophys. Acta, 1076, 86-90.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Escherichia coli

Protein Variants

Protein Variants Comment Organism
H246D His246alpha to Asp mutant is indistinguishable from the native enzyme with respect to its subunit assembly, but has no ability to catalyze the overall reaction. The mutant enzyme is incapable of undergoing phosphorylation and is devoid of arsenolysis activity Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
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additional information
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Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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His246alpha to Asp mutant
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + succinate + CoA
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Escherichia coli ADP + phosphate + succinyl-CoA
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