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Literature summary for 3.5.1.22 extracted from

  • Kalvero Airas, R.
    Kinetic study on the reaction mechanism of pantothenase:Existence of an acyl-enzyme intermediate and role of general acid catalysis (1978), Biochemistry, 17, 4932-4939.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
m-aminophenylboronic acid competitive inhibition Pseudomonas fluorescens
Phenylmethanesulfonylfluoride
-
Pseudomonas fluorescens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
8 16 pantothenic acid pH dependent Pseudomonas fluorescens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pantothenic acid + H2O Pseudomonas fluorescens
-
?
-
?

Organism

Organism UniProt Comment Textmining
Pseudomonas fluorescens
-
NCIB12017, earlier Pseudomonas fluorescens UK-1, isolated from sea water
-

Purification (Commentary)

Purification (Comment) Organism
-
Pseudomonas fluorescens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
7.2
-
-
Pseudomonas fluorescens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pantothenic acid + H2O
-
Pseudomonas fluorescens beta-alanine + D-pantoyl lactone + H2O
-
r
pantothenic acid + H2O
-
Pseudomonas fluorescens ?
-
?

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
10 30
-
Pseudomonas fluorescens