We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Information on EC 3.5.1.22 - pantothenase for references in articles please use BRENDA:EC3.5.1.22
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
pantothenate hydrolase,
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pantothenate hydrolase
-
-
pantothenate hydrolase
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(R)-pantothenate + H2O = (R)-pantoate + beta-alanine
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
hydrolysis of peptide bond
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(R)-pantothenate amidohydrolase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pantothenate + H2O
2,4-dihydroxy-3,3-dimethylbutyric acid + beta-alanine
-
-
-
-
?
pantothenic acid + H2O
beta-alanine + D-pantoic acid
pantothenic acid + H2O
beta-alanine + D-pantoyl lactone
pantoyl-gamma-aminobutyrate + H2O
4-aminobutyrate + D-pantoate
-
-
-
-
?
pantothenic acid + H2O
?
-
-
-
-
-
pantothenic acid + H2O
?
-
sole source of carbon and nitrogen
-
-
-
pantothenic acid + H2O
?
-
-
-
-
-
pantothenic acid + H2O
beta-alanine + D-pantoic acid
-
-
-
ir
pantothenic acid + H2O
beta-alanine + D-pantoic acid
-
PS-21
-
ir
pantothenic acid + H2O
beta-alanine + D-pantoic acid
-
PS-21
-
ir
pantothenic acid + H2O
beta-alanine + D-pantoyl lactone
-
-
-
-
?
pantothenic acid + H2O
beta-alanine + D-pantoyl lactone
-
-
-
-
?
pantothenic acid + H2O
beta-alanine + D-pantoyl lactone
-
-
-
-
-
pantothenic acid + H2O
beta-alanine + D-pantoyl lactone
-
-
-
-
r
pantothenic acid + H2O
beta-alanine + D-pantoyl lactone
-
-
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pantothenic acid + H2O
?
-
-
-
-
-
pantothenic acid + H2O
?
-
sole source of carbon and nitrogen
-
-
-
pantothenic acid + H2O
?
-
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Phenylmethanesulfonylfluoride
SO42-
-
only strain PS-21
m-aminophenylboronic acid
-
competitive inhibition
m-aminophenylboronic acid
-
-
oxalate
-
same ligands inhibits enzyme act as effective protectors against thermal inactivation
oxaloacetate
-
carboxyclic acids, especially 2-oxo-carboxylic acids
oxaloacetate
-
noncompetitive inhibition, dependent on pH
Phenylmethanesulfonylfluoride
-
-
Phenylmethanesulfonylfluoride
-
strain PS-21 not inhibited
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3.2 - 24
pantothenic acid
3.2
pantothenic acid
-
PS-21, pH 8.1, 50 mM diethanolamine/H2SO4, Km-value pH independent
5
pantothenic acid
-
P-2, pH 7.5 at 28°C
5
pantothenic acid
-
P-2, pH 7.4 at 28°C
7.6
pantothenic acid
-
pH-independent theoretical Km
8 - 16
pantothenic acid
-
pH dependent
12.5
pantothenic acid
-
60 mM potassium phosphate, pH 7.4
13
pantothenic acid
-
20 mM potassium phosphate, pH 7.4
15
pantothenic acid
-
dependent on pH, phosphate buffer, pH 7.0, 20°C
15
pantothenic acid
-
5 mM potassium phosphate, pH 7.4
18
pantothenic acid
-
10 mM sodium diphosphate/H2SO4, pH 7.5
22
pantothenic acid
-
10 mM Tris/H2SO4, pH 7.5
24
pantothenic acid
-
10 mM Tris/10 mM citric acid(KOH), pH 7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
28 - 29
-
above 30°C denaturation of enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
NCIB 6990
-
-
brenda
P-2
-
-
brenda
PS-21
-
-
brenda
-
-
-
brenda
biotype C; NCIB12017, earlier Pseudomonas fluorescens UK-1, isolated from sea water; P-2
-
-
brenda
NCIB12017, earlier Pseudomonas fluorescens UK-1, isolated from sea water
-
-
brenda
NCIB12017, earlier Pseudomonas fluorescens UK-1, isolated from sea water; P-2
-
-
brenda
NCIB12017, earlier Pseudomonas fluorescens UK-1, isolated from sea water; PS-21
-
-
brenda
P-2
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
50000
-
2 * 50000, SDS-PAGE
58500
-
4 * 58500, strain PS-21, SDS-PAGE
240000
-
PS-21, gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dimer
-
2 * 50000, SDS-PAGE
dimer
-
2 * 50000, SDS-PAGE
-
tetramer
-
4 * 58500, strain PS-21, SDS-PAGE
tetramer
-
4 * 58500, strain PS-21, SDS-PAGE
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5.5 - 10
-
below pH 5 activity rapidly decreases
171982
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
28 - 37
-
partial inactivation, reactivation with oxalate, oxaloacetate or pyruvate to 10-20% of original activity, 30 min at 35°, inactivation
30 - 35
-
above 30°C rapidly inactivated, at 35°C inactivation rate 7.2%/min
28 - 40
-
heat inactivation occurs above 28°C, inactivated at 40°C
28 - 40
-
thermal inactivation, reactivation when temperature is lowered again
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-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%
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
nutrition
-
vitamin determination, extremely sensitive assay of pantothenic acid in various dietary sources, as low as 5 nM concentration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Lactobacillus 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
Select items on the left to see more content.
html completed
HOME
login
history
all enzymes
BRENDA home
History
3.5.1.22 pantothenase
more
top
Information
