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Information on EC 3.5.99.7 - 1-aminocyclopropane-1-carboxylate deaminase and Organism(s) Rhizobium leguminosarum bv. viciae and UniProt Accession Q93AG0

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IUBMB Comments
A pyridoxal 5'-phosphate enzyme. The enzyme, found in certain soil bacteria and fungi, catalyses the ring opening of 1-aminocyclopropane-1-carboxylate, the immediate precursor to ethylene, an important plant hormone that regulates fruit ripening and other processes. The enzyme releases an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. The enzyme has been used to make fruit ripening dependent on externally added ethylene, as it removes the substrate for endogenous ethylene formation.
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Rhizobium leguminosarum bv. viciae
UNIPROT: Q93AG0
Word Map
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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Synonyms
1-aminocyclopropane-1-carboxylate deaminase, 1-aminocyclopropane-1-carboxylate endolyase (deaminating), 1-aminocyclopropane-1-carboxylic acid deaminase, 1-aminocyclopropane-1-carboxylic acid-deaminase, ACC deaminase, ACC-deaminase, ACCD, ACD, AcdS, ACPC deaminase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1-aminocyclopropane-1-carboxylate endolyase (deaminating)
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1-aminocyclopropane-1-carboxylic acid deaminase
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ACC deaminase
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ACPC deaminase
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deaminase, 1-aminocyclopropane-1-carboxylate
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
1-aminocyclopropane-1-carboxylate aminohydrolase (isomerizing)
A pyridoxal 5'-phosphate enzyme. The enzyme, found in certain soil bacteria and fungi, catalyses the ring opening of 1-aminocyclopropane-1-carboxylate, the immediate precursor to ethylene, an important plant hormone that regulates fruit ripening and other processes. The enzyme releases an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. The enzyme has been used to make fruit ripening dependent on externally added ethylene, as it removes the substrate for endogenous ethylene formation.
CAS REGISTRY NUMBER
COMMENTARY hide
69553-48-6
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
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