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Literature summary extracted from

  • Thibodeaux, C.J.; Liu, H.W.
    Mechanistic studies of 1-aminocyclopropane-1-carboxylate deaminase: characterization of an unusual pyridoxal 5-phosphate-dependent reaction (2011), Biochemistry, 50, 1950-1962.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.99.7 wild-type enzyme and mutants Y268F and Y294F as His6-tagged proteins in Escherichia coli Pseudomonas sp.

Protein Variants

EC Number Protein Variants Comment Organism
3.5.99.7 E295D site-directed mutagesis, mutant kinetics compared to the wild-type, overview Pseudomonas sp.
3.5.99.7 Y268F site-directed mutagesis, mutant kinetics compared to the wild-type, overview Pseudomonas sp.
3.5.99.7 Y294F site-directed mutagesis, mutant kinetics compared to the wild-type, overview Pseudomonas sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.99.7 additional information
-
 additional information steady-state kinetics and pH-dependence, overview Pseudomonas sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.99.7 1-aminocyclopropane-1-carboxylate + H2O Pseudomonas sp.
-
 2-oxobutanoate + NH3
-
 ?
3.5.99.7 1-aminocyclopropane-1-carboxylate + H2O Pseudomonas sp. ACP
-
 2-oxobutanoate + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.99.7 Pseudomonas sp.
-
-
-
3.5.99.7 Pseudomonas sp. ACP
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.5.99.7 1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3 reaction mechanism, detailed overview Pseudomonas sp.
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.99.7 1-aminocyclopropane-1-carboxylate + H2O
-
 Pseudomonas sp. 2-oxobutanoate + NH3
-
 ?
3.5.99.7 1-aminocyclopropane-1-carboxylate + H2O the pyridoxal 5'-phosphate-dependent enzyme cleaves the cyclopropane ring of ACC, to give 2-oxobutyric acid and ammonia as products. The pKa of the conserved active site residue, Tyr294, is lowered by a hydrogen bonding interaction with a second conserved residue, Tyr268. This allows Tyr294 to deprotonate the incoming amino group of ACC to initiate the aldimine exchange reaction between ACC and the pyridoxal 5'-phosphate coenzyme and also likely helps to activate Tyr294 for a role as a nucleophile to attack and cleave the cyclopropane ring of the substrate. The Calpha-Cbeta bond cleavage step in the chemical mechanism is at least partially rate-limiting under kcat/Km conditions and is likely preceded in the mechanism by a partially rate-limiting step involving the conversion of a stable gem-diamine intermediate into a reactive external aldimine intermediate that is poised for cyclopropane ring cleavage Pseudomonas sp. 2-oxobutanoate + NH3
-
 ?
3.5.99.7 1-aminocyclopropane-1-carboxylate + H2O
-
 Pseudomonas sp. ACP 2-oxobutanoate + NH3
-
 ?
3.5.99.7 1-aminocyclopropane-1-carboxylate + H2O the pyridoxal 5'-phosphate-dependent enzyme cleaves the cyclopropane ring of ACC, to give 2-oxobutyric acid and ammonia as products. The pKa of the conserved active site residue, Tyr294, is lowered by a hydrogen bonding interaction with a second conserved residue, Tyr268. This allows Tyr294 to deprotonate the incoming amino group of ACC to initiate the aldimine exchange reaction between ACC and the pyridoxal 5'-phosphate coenzyme and also likely helps to activate Tyr294 for a role as a nucleophile to attack and cleave the cyclopropane ring of the substrate. The Calpha-Cbeta bond cleavage step in the chemical mechanism is at least partially rate-limiting under kcat/Km conditions and is likely preceded in the mechanism by a partially rate-limiting step involving the conversion of a stable gem-diamine intermediate into a reactive external aldimine intermediate that is poised for cyclopropane ring cleavage Pseudomonas sp. ACP 2-oxobutanoate + NH3
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.99.7 ACC deaminase
-
 Pseudomonas sp.
3.5.99.7 ACCD
-
 Pseudomonas sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.99.7 25
-
 assay at Pseudomonas sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.99.7 additional information
-
 steady-state kinetics and pH-dependence, overview Pseudomonas sp.
3.5.99.7 7.5
-
 assay at for wild-type enzyme and mutants E295D and Y294F Pseudomonas sp.
3.5.99.7 8.8
-
 assay at for mutant Y268F Pseudomonas sp.

Cofactor

EC Number Cofactor Comment Organism Structure
3.5.99.7 pyridoxal 5'-phosphate dependent on Pseudomonas sp.