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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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EC Tree
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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This record set is specific for:
Rhizobium leguminosarum bv. viciae
UNIPROT: Q93AG0
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Word Map
The taxonomic range for the selected organisms is: Rhizobium leguminosarum bv. viciae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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Synonyms
acc deaminase, 1-aminocyclopropane-1-carboxylate deaminase, acc-deaminase, 1-aminocyclopropane-1-carboxylic acid deaminase, 1-aminocyclopropane-1-carboxylic acid-deaminase, 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
LOCALIZATION PREDICTION?
1A1D_RHILV
339
0
36607
Swiss-Prot
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