Information on EC 3.5.1.22 - pantothenase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
3.5.1.22
-
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RECOMMENDED NAME
GeneOntology No.
pantothenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-pantothenate + H2O = (R)-pantoate + beta-alanine
show the reaction diagram
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Pantothenate and CoA biosynthesis
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
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SYSTEMATIC NAME
IUBMB Comments
(R)-pantothenate amidohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9076-90-8
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
NCIB 6990
-
-
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
pantothenate + H2O
2,4-dihydroxy-3,3-dimethylbutyric acid + beta-alanine
show the reaction diagram
-
-
-
-
?
pantothenic acid + H2O
?
show the reaction diagram
pantothenic acid + H2O
beta-alanine + D-pantoic acid
show the reaction diagram
pantothenic acid + H2O
beta-alanine + D-pantoyl lactone
show the reaction diagram
pantoyl-gamma-aminobutyrate + H2O
4-aminobutyrate + D-pantoate
show the reaction diagram
-
-
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
pantothenic acid + H2O
?
show the reaction diagram
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
chloroamphenicol
-
-
di-isopropylphosphofluoridate
-
strain PS-21 not inhibited
dieethyldithiocarbamate
-
10 mM, 36% inhibition
EDTA
-
10 mM, 45% inhibition
KCN
-
10 mM, 42% inhibition
m-aminophenylboronic acid
oxalate
oxaloacetate
Phenylmethanesulfonylfluoride
SO42-
-
only strain PS-21
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.2 - 24
pantothenic acid
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13.7
-
strain PS-21
86.9
-
strain P-2
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
strain P-2
9 - 9.2
-
strain PS-21
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28 - 29
-
above 30°C denaturation of enzyme
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
-
2 * 50000, SDS-PAGE
58500
-
4 * 58500, strain PS-21, SDS-PAGE
97400
-
gel filtration
100000
-
gel filtration
240000
-
PS-21, gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 10
-
below pH 5 activity rapidly decreases
171982
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28 - 37
-
partial inactivation, reactivation with oxalate, oxaloacetate or pyruvate to 10-20% of original activity, 30 min at 35°, inactivation
28 - 40
30 - 35
-
above 30°C rapidly inactivated, at 35°C inactivation rate 7.2%/min
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C 20 mM potassium phosphate pH 7, enzyme is made accessible to substrates by freezing and thawing four times, decrease of activity 20% per round of freezing and thawing, frozen enzyme retains activity for at least 2 years
-
-20°C 35 mM potassium phosphate, pH 6.8
-
-20°C enzyme is stable frozen, but loses activity in solution at 0°C in a few days
-
-20°C, 5 mM K2SO4, repeated cycles of freezing and thawing inactivate the enzyme
-
2°C 5 mM K2SO4, 1 week, activity dimished to 50%
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nutrition
-
vitamin determination, extremely sensitive assay of pantothenic acid in various dietary sources, as low as 5 nM concentration
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LINKS TO OTHER DATABASES (specific for EC-Number 3.5.1.22)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)