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Literature summary for 6.4.1.1 extracted from

  • Lietzan, A.D.; Lin, Y.; St Maurice, M.
    The role of biotin and oxamate in the carboxyltransferase reaction of pyruvate carboxylase (2014), Arch. Biochem. Biophys., 562, 70-79 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.4.1.1

Cloned(Commentary)

Cloned (Comment) Organism
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 Rhizobium etli

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of the carboxyltransferase domain, to 2.26-2.4 A resolution. Oxamate is positioned in the active site in an identical manner to the substrate, pyruvate Rhizobium etli

Protein Variants

Protein Variants Comment Organism
additional information construction of deletion mutants lacking the biotin carboxylase domain or both biotin carboxylase and biotin carboxyl carrier domains. The biotin carboxyl carrier domain devoid of biotin does not contribute directly to the enzymatic reaction, a deletion mutant demonstrates biotin-independent oxaloacetate decarboxylation activity Rhizobium etli

Organism

Organism UniProt Comment Textmining
Rhizobium etli Q2K340
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Rhizobium etli ATCC 51251 Q2K340
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information in the absence of the biotin carboxylase domain, oxamate-stimulated decarboxylation of oxaloacetate, reaction of EC 4.1.1.3, proceeds through a simple ping-pong bi bi mechanism Rhizobium etli ?
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 ?
additional information in the absence of the biotin carboxylase domain, oxamate-stimulated decarboxylation of oxaloacetate, reaction of EC 4.1.1.3, proceeds through a simple ping-pong bi bi mechanism Rhizobium etli ATCC 51251 ?
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 ?

Synonyms

Synonyms Comment Organism
PYC
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 Rhizobium etli