Literature summary 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.

Inhibitors

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

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
3.5.1.22	8	16	pantothenic acid	pH dependent	Pseudomonas fluorescens

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

EC Number	Purification (Comment)	Organism
3.5.1.22	-	Pseudomonas fluorescens

Specific Activity [micromol/min/mg]

EC Number	Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
3.5.1.22	7.2	-	-	Pseudomonas fluorescens

Substrates and Products (Substrate)

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

Temperature Range [°C]

EC Number	Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
3.5.1.22	10	30	-	Pseudomonas fluorescens

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Release 2023.1 (January 2023)