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Information on EC 3.4.13.9 - Xaa-Pro dipeptidase

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.13 Dipeptidases
                3.4.13.9 Xaa-Pro dipeptidase
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This record set is specific for:
UNIPROT: O58691 not found.
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
hydrolysis of Xaa-/-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-Pro
hydrolysis of Xaa-/-Pro dipeptides; also acts on aminoacyl-hydroxyamine analogues. No action on Pro-Pro
Synonyms
prolidase, serum prolidase, peptidase d, prolidase i, organophosphorus acid anhydrolase, proline dipeptidase, prolidase ii, imidodipeptidase, quiescent cell proline dipeptidase, prolyl dipeptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PH0974
locus name
dipeptidase, proline
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-
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gamma-peptidase
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imidodipeptidase
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-
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peptidase D
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-
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prolidase
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-
-
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Proline dipeptidase
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X-Pro dipeptidase
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CAS REGISTRY NUMBER
COMMENTARY hide
9025-32-5
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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
Ala-Pro + H2O
Ala + Pro
show the reaction diagram
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-
-
?
Gly-Pro + H2O
Gly + Pro
show the reaction diagram
-
-
-
?
Leu-Pro + H2O
Leu + Pro
show the reaction diagram
-
-
-
?
Met-Pro + H2O
Met + Pro
show the reaction diagram
-
-
-
?
Phe-Pro + H2O
Phe + Pro
show the reaction diagram
-
-
-
?
Val-Pro + H2O
Val + Pro
show the reaction diagram
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-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.81 - 2.92
Leu-Pro
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1079 - 2861
Leu-Pro
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
980 - 2049
Leu-Pro
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1119
substrate: Leu-Pro, pH 7.0, 70°C, mutant enzyme E127G/E252D
1245
substrate: Leu-Pro, pH 7.0, 70°C, mutant enzyme A195T/G306S
1597
substrate: Leu-Pro, pH 7.0, 70°C, mutant enzyme E36V
2146
substrate: Leu-Pro, pH 7.0, 70°C, mutant enzyme Y301C/K342N
809
substratwe: Leu-Pro, pH 7.0, 70°C, wild-type enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
wild-type enzyme and mutant enzymes A195T/G306S, Y301C/K342N, E127G/E252D and E36V
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
O58691_PYRHO
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
356
0
40175
TrEMBL
other Location (Reliability: 3)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A195T/G306S
mutation causes an increase in Tm-value of 0.1°C. Mutation causes an 1.7fold increase of the catalytic efficiency towards Leu-Pro
E127G/E252D
mutation causes an decrease in Tm-value of 2.1°C. Mutation causes an 1.3fold increase of the catalytic efficiency towards Leu-Pro
E36V
mutation causes an increase in Tm-value of 0.6°C. Mutation causes an 1.1fold increase of the catalytic efficiency towards Leu-Pro
Y301C/K342N
mutation causes an decrease in Tm-value of 0.5°C. Mutation causes an 1.2fold decrease of the catalytic efficiency towards Leu-Pro
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
112
Tm-value for mutant enzyme E127G/E252D is 112.2°C
114
Tm-value for wild-type enzyme is 114.3°C, Tm-value for mutant enzyme A195T/G306S is 114.4°C, Tm-value for mutant enzyme Y301C/K342N is 113.8°C
115
Tm-value for mutant enzyme E36V is 112.2°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type enzyme and mutant enzymes A195T/G306S, Y301C/K342N, E127G/E252D and E36V
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Theriot, C.M.; Semcer, R.L.; Shah, S.S.; Grunden, A.M.
Improving the catalytic activity of hyperthermophilic Pyrococcus horikoshii prolidase for detoxification of organophosphorus nerve agents over a broad range of temperatures
Archaea
2011
565127
2011
Pyrococcus horikoshii (O58691), Pyrococcus horikoshii, Pyrococcus horikoshii DSM 12428 (O58691)
Manually annotated by BRENDA team