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Literature summary for 3.5.1.11 extracted from

  • Kumar, A.; Gowda, N.; Gaikwad, S.; Pundle, A.
    Rhodotorula aurantiaca penicillin V acylase: active site characterization and fluorometric studies (2009), J. Photochem. Photobiol. B, 97, 109-116.
    View publication on PubMed

Application

Application Comment Organism
synthesis PVA is a pharmaceutically important enzyme to produce 6-aminopenicillanic acid Buckleyzyma aurantiaca

Inhibitors

Inhibitors Comment Organism Structure
N-bromosuccinimide
-
Buckleyzyma aurantiaca
Phenylmethylsulfonylfluoride
-
Buckleyzyma aurantiaca

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
penicillin V + H2O Buckleyzyma aurantiaca
-
phenoxyacetate + 6-aminopenicillinate
-
?

Organism

Organism UniProt Comment Textmining
Buckleyzyma aurantiaca
-
NCIM 3425
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
penicillin V + H2O
-
Buckleyzyma aurantiaca phenoxyacetate + 6-aminopenicillinate
-
?
penicillin V + H2O involvement of serine and tryptophan in the enzyme activity Buckleyzyma aurantiaca phenoxyacetate + 6-aminopenicillinate
-
?

Subunits

Subunits Comment Organism
More penicillin acylases share a common structural fold and possess a catalytic serine or cysteine or threonine residue at the N-terminal end Buckleyzyma aurantiaca

Synonyms

Synonyms Comment Organism
More PVA is a member of the N-terminal nucleophile, Ntn, hydrolase superfamily Buckleyzyma aurantiaca
penicillin V acylase
-
Buckleyzyma aurantiaca
PVA
-
Buckleyzyma aurantiaca

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
additional information inhibition kinetics, effects of tryptophan and serine modifications by phenylmethylsulfonylfluoride and N-bromosuccinimide, fluorometric studies, overview Buckleyzyma aurantiaca