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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
pantothenate hydrolase,
more
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pantothenate hydrolase
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pantothenate hydrolase
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(R)-pantothenate + H2O = (R)-pantoate + beta-alanine
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hydrolysis of peptide bond
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(R)-pantothenate amidohydrolase
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pantothenate + H2O
2,4-dihydroxy-3,3-dimethylbutyric acid + beta-alanine
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pantothenic acid + H2O
beta-alanine + D-pantoic acid
pantothenic acid + H2O
beta-alanine + D-pantoyl lactone
pantoyl-gamma-aminobutyrate + H2O
4-aminobutyrate + D-pantoate
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pantothenic acid + H2O
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pantothenic acid + H2O
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sole source of carbon and nitrogen
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pantothenic acid + H2O
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pantothenic acid + H2O
beta-alanine + D-pantoic acid
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ir
pantothenic acid + H2O
beta-alanine + D-pantoic acid
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PS-21
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ir
pantothenic acid + H2O
beta-alanine + D-pantoic acid
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PS-21
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pantothenic acid + H2O
beta-alanine + D-pantoyl lactone
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pantothenic acid + H2O
beta-alanine + D-pantoyl lactone
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pantothenic acid + H2O
beta-alanine + D-pantoyl lactone
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pantothenic acid + H2O
beta-alanine + D-pantoyl lactone
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r
pantothenic acid + H2O
beta-alanine + D-pantoyl lactone
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r
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pantothenic acid + H2O
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pantothenic acid + H2O
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sole source of carbon and nitrogen
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pantothenic acid + H2O
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di-isopropylphosphofluoridate
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strain PS-21 not inhibited
dieethyldithiocarbamate
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10 mM, 36% inhibition
EDTA
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10 mM, 45% inhibition
KCN
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10 mM, 42% inhibition
m-aminophenylboronic acid
Phenylmethanesulfonylfluoride
SO42-
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only strain PS-21
m-aminophenylboronic acid
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competitive inhibition
m-aminophenylboronic acid
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oxalate
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oxalate
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same ligands inhibits enzyme act as effective protectors against thermal inactivation
oxaloacetate
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oxaloacetate
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carboxyclic acids, especially 2-oxo-carboxylic acids
oxaloacetate
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noncompetitive inhibition, dependent on pH
oxaloacetate
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noncompetitive inhibition, dependent on pH
Phenylmethanesulfonylfluoride
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Phenylmethanesulfonylfluoride
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strain PS-21 not inhibited
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3.2 - 24
pantothenic acid
3.2
pantothenic acid
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PS-21, pH 8.1, 50 mM diethanolamine/H2SO4, Km-value pH independent
5
pantothenic acid
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P-2, pH 7.4 at 28°C
5
pantothenic acid
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P-2, pH 7.5 at 28°C
7.6
pantothenic acid
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pH-independent theoretical Km
8 - 16
pantothenic acid
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pH dependent
12.5
pantothenic acid
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60 mM potassium phosphate, pH 7.4
13
pantothenic acid
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20 mM potassium phosphate, pH 7.4
15
pantothenic acid
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5 mM potassium phosphate, pH 7.4
15
pantothenic acid
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dependent on pH, phosphate buffer, pH 7.0, 20°C
18
pantothenic acid
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10 mM sodium diphosphate/H2SO4, pH 7.5
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pantothenic acid
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10 mM Tris/H2SO4, pH 7.5
24
pantothenic acid
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10 mM Tris/10 mM citric acid(KOH), pH 7.5
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28 - 29
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above 30°C denaturation of enzyme
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brenda
NCIB 6990
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brenda
P-2
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brenda
PS-21
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brenda
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brenda
biotype C
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brenda
NCIB12017, earlier Pseudomonas fluorescens UK-1, isolated from sea water
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brenda
P-2
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brenda
PS-21
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brenda
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brenda
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240000
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PS-21, gel filtration
50000
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2 * 50000, SDS-PAGE
58500
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4 * 58500, strain PS-21, SDS-PAGE
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dimer
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2 * 50000, SDS-PAGE
dimer
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2 * 50000, SDS-PAGE
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tetramer
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4 * 58500, strain PS-21, SDS-PAGE
tetramer
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4 * 58500, strain PS-21, SDS-PAGE
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5.5 - 10
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below pH 5 activity rapidly decreases
171982
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28 - 37
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partial inactivation, reactivation with oxalate, oxaloacetate or pyruvate to 10-20% of original activity, 30 min at 35°, inactivation
30 - 35
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above 30°C rapidly inactivated, at 35°C inactivation rate 7.2%/min
28 - 40
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heat inactivation occurs above 28°C, inactivated at 40°C
28 - 40
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thermal inactivation, reactivation when temperature is lowered again
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-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
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-20°C 35 mM potassium phosphate, pH 6.8
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-20°C enzyme is stable frozen, but loses activity in solution at 0°C in a few days
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-20°C, 5 mM K2SO4, repeated cycles of freezing and thawing inactivate the enzyme
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2°C 5 mM K2SO4, 1 week, activity dimished to 50%
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nutrition
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vitamin determination, extremely sensitive assay of pantothenic acid in various dietary sources, as low as 5 nM concentration
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Kalvero Airas, R.
Pantothenase-based assay of pantothenic acid
Methods Enzymol.
122
33-35
1986
Pseudomonas fluorescens
brenda
Kalvero Airas, R.
Pantothenase-based assay of pantothenic acid
Anal. Biochem.
134
122-125
1983
Pseudomonas fluorescens
brenda
Kalvero Airas, R.
Pantothenase from Pseudomonas fluorescens
Methods Enzymol.
62
267-275
1979
Pseudomonas fluorescens
brenda
Solberg, O.; Hegma, I.K.
Microbiological assay of pantothenic acid
Methods Enzymol.
62
201-205
1979
Lactiplantibacillus plantarum, Pediococcus acidilactici
brenda
Kalvero Airas, R.
Kinetic study on the reaction mechanism of pantothenase:Existence of an acyl-enzyme intermediate and role of general acid catalysis
Biochemistry
17
4932-4939
1978
Pseudomonas fluorescens
brenda
Kalvero Airas, R.
On the partial reactivation of inactivated pantothenase from Pseudomonas fluorescens
Biochim. Biophys. Acta
452
201-208
1976
Pseudomonas fluorescens
brenda
Kalvero Airas, R.
Thermal inactivation of pantothenase from Pseudomonas fluorescens
Biochim. Biophys. Acta
452
193-200
1976
Pseudomonas fluorescens
brenda
Kalvero Airas, R.
Kinetic studies on pantothenase of Pseudomonas fluorescens
Biochem. J.
157
415-421
1976
Pseudomonas fluorescens, Pseudomonas fluorescens P-2
brenda
Kalvero Airas, R.; Hietanen, E.A.; Nurmikko, V.T.
Purification and properties of pantothenase from Pseudomonas fluorescens
Biochem. J.
157
409-413
1976
Pseudomonas fluorescens, Pseudomonas fluorescens P-2
brenda
Kalvero Airas, R.
Thermal inactivation and reactivation of an enzyme in vivo
Biochem. J.
130
111-119
1972
Pseudomonas fluorescens
brenda
Nurmikko, V.; Salo, E.; Hakkola, H.; Maekinen, K.; Snell, E.E.
The bacterial degradation of pantothenic acid. II. pantothenate hydrolase
Biochemistry
5
399-403
1966
Pseudomonas fluorescens, Pseudomonas fluorescens P-2
brenda
Kalvero Airas, R.
Pantothenases from pseudomonads produce either pantoyl lactone or pantoic acid
Biochem. J.
250
447-451
1988
Pseudomonas fluorescens, Pseudomonas fluorescens PS-21
brenda
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