3.4.13.9: Xaa-Pro dipeptidase
This is an abbreviated version!
For detailed information about Xaa-Pro dipeptidase, go to the full flat file.
Word Map on EC 3.4.13.9
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3.4.13.9
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collagen
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dipeptides
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ulcer
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hydroxyproline
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gly-pro
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opaas
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soman
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exopeptidase
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proline-containing
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prolinase
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map-kinases
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paraoxonase
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dfp
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igf-ir
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alteromonas
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erk1
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splenomegaly
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sarin
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medicine
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beta1-integrin
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analysis
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diagnostics
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drug development
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degradation
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biotechnology
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food industry
- 3.4.13.9
- collagen
- dipeptides
- ulcer
- hydroxyproline
- gly-pro
-
opaas
- soman
-
exopeptidase
-
proline-containing
- prolinase
-
map-kinases
- paraoxonase
- dfp
- igf-ir
- alteromonas
- erk1
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splenomegaly
- sarin
- medicine
- beta1-integrin
- analysis
- diagnostics
- drug development
- degradation
- biotechnology
- food industry
Reaction
hydrolysis of Xaa-/-Pro dipeptides; also acts on aminoacyl-hydroxyamine analogues. No action on Pro-Pro =
Synonyms
clan MG aminopeptidase P-like metallopeptidase, dipeptidase, proline, DPP8, EC 3.4.3.7, gamma-peptidase, imidodipeptidase, LGAS_0712, M24B peptidase, More, MP50, OPAA, OPAA-2, organophosphate acid anhydrolase, organophosphate anhydrolase/prolidase, organophosphorus acid anhydrolase, PepD, PepE, PepI, PepQ, peptidase D, peptidase-Q, PepX, Pf-peptidase, Pfprol, PH0974, PH1149, Ph1prol, Phprol, PLD, post-proline-cleaving aminopeptidase, prolidase, prolidase homolog 1, prolidase homolog 2, prolidase I, prolidase II, Proline dipeptidase, proline iminopeptidase, proline-specific amino dipeptidase, prolyl dipeptidase, PRS, QPP, quiescent cell proline dipeptidase, serum prolidase, X-Pro dipeptidase, X-prolyl-dipeptidyl aminopeptidase, Xaa-Pro dipeptidase, XPD, XPD43, XPP
ECTree
3.4.13.9 Xaa-Pro dipeptidaseAdvanced search results
results (
results (Engineering
Engineering on EC 3.4.13.9 - Xaa-Pro dipeptidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
R46A
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two orders of magnitude loss in the enzymatic activity for all the dipeptides attempted. The Glu340 side-chain interacts with Arg46 and stabilizes its side-chain conformation that is appropriate for substrate binding
F822A
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
H859A
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
S202F
V833A
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
Y231del
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homozygous mutation observed in two unrelated patients with enzyme deficiency. Mutation results in loss of enzyme activity in skin fibroblasts. Long-term cultured fibroblasts bearing the mutant accumulate Gly-L-Pro dipeptide intracellularly
Y256X
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a homozygous nonsense C > G transition at nucleotide 768 is a naturally occuring mutation, which leads to recalcitrant leg ulceration, splenomegaly, and photosensitive rash due to prolidase deficiency, phenotype, overview
Y844A
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
L193E
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site-directed mutagenesis, the mutant is active on Pro-Pro in contrast to the wild-type enzyme, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme
L193E/V302D
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site-directed mutagenesis, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme
L193R
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site-directed mutagenesis, the mutation in the S1 site eliminates the allosteric behaviour of the enzyme, the mutant is active on Pro-Pro and Gly-Pro in presence of zinc ions in contrast to the wild-type enzyme, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme
L193R/V302D
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site-directed mutagenesis, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme
L193T
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site-directed mutagenesis, the mutant is active on Pro-Pro and Gly-Pro in contrast to the wild-type enzyme, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme
R293S
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the mutation results in the disappearance of the allosteric behaviour yielding a Hill constant of 0.98 while the wild type has a constant of 1.58 and suppresses the substrate inhibition that is observed in other mutants and wild type enzyme, the Km value for L-Leu-L-Pro is 2.9fold larger and Vmax is approximately 50% less as compared to the wild type enzyme
R293S/S307G
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mutant shows strongly reduced specific activity towards L-Leu-L-Pro compared to the wild type enzyme
S307D
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mutant shows reduced specific activity towards L-Leu-L-Pro compared to the wild type enzyme
S307G
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mutant shows reduced specific activity towards L-Leu-L-Pro compared to the wild type enzyme
S307R
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mutant shows reduced specific activity towards L-Leu-L-Pro compared to the wild type enzyme
V302D
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site-directed mutagenesis, the mutation in the S1 site eliminates the allosteric behaviour of the enzyme. The mutant is active on Pro-Pro in presence of zinc ions in contrast to the wild-type enzyme, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme
V302K
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site-directed mutagenesis, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme
V302T
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site-directed mutagenesis, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme
D209A
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less than 0.1% enzymic activity, contains 0.7 Co per subunit, maximal activity with 0.5 mM Co2+, less than 20% residual activity with 10 mM Co2+
E313L
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protein is highly misfolded, remains aggregated and recalcitrant during purification
G39E
H284L
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less than 0.1% enzymic activity, contains 0.28 Co per subunit. Inhibitory effect of high Co2+-concentration is less pronounced than in wild-type
R19G/G39E/K71E/S229T
R19G/K71E/S229
site-directed mutagenesis, the mutant shows altered kinetics and temperature profile
R19G/K71E/S229T
mutant enzyme shows a higher activity than wild-type enzyme over a broad range of temperatures, the thermostability of the mutant enzymes is less compared to wild type. At 35°C, 70°C and 100°C the mutant exhibits higher Vmax and kcat values than wild-type prolidase for Met-Pro. kcat/Km for Met-Pro is 1.1fold higher than wild-type value at 35°C, kcat/Km for Met -Pro comparable to wild-type value at 70°C, kcat/Km for Met-Pro is 2.4fold higher than wild-type value at 100°C. Relative specific activity towards Met-Pro at 100°C is 137% of wild-type activity. Relative specific activity towards Leu-Pro at 100°C is 169% of wild-type activity. Relative specific activity towards Phe-Pro at 100°C is 97% of wild-type activity. Relative specific activity towards Ala-Pro at 100°C is 95% of wild-type activity. Relative specific activity towards Gly-Pro at 100°C is 47% of wild-type activity. Relative specific activity towards Arg-Pro at 100°C is 101% of wild-type activity. Catalytic activity of the mutant enzyme has similar response to changes in pH as wild-type enzyme and shows optimal activity at pH 7.0, although the activity is 89% of wild-type activity
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
A195T/G306S
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mutation causes an increase in Tm-value of 0.1°C. Mutation causes an 1.7fold increase of the catalytic efficiency towards Leu-Pro
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E127G/E252D
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mutation causes an decrease in Tm-value of 2.1°C. Mutation causes an 1.3fold increase of the catalytic efficiency towards Leu-Pro
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E36V
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mutation causes an increase in Tm-value of 0.6°C. Mutation causes an 1.1fold increase of the catalytic efficiency towards Leu-Pro
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Y301C/K342N
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mutation causes an decrease in Tm-value of 0.5°C. Mutation causes an 1.2fold decrease of the catalytic efficiency towards Leu-Pro
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additional information
G39E
site-directed mutagenesis, the mutant shows altered kinetics and temperature profile
G39E
at 35°C, 70°C and 100°C the mutant exhibits higher Vmax and kcat values than wild-type prolidase for Met-Pro. kcat/Km for Met-Pro is 70% of wild-type value at 35°C, kcat/Km for Met-Pro is 80% of wild-type value at 70°C, kcat/Km for Met-Pro is 1.2fold higher than wild-type value at 100°C. Relative specific activity towards Met-Pro at 100°C is 103% of wild-type activity. Relative specific activity towards Leu-Pro at 100°C is 85% of wild-type activity. Relative specific activity towards Phe-Pro at 100°C is 60% of wild-type activity. Relative specific activity towards Ala-Pro at 100°C is 35% of wild-type activity. Relative specific activity towards Gly-Pro at 100°C is 37% of wild-type activity. Relative specific activity towards Arg-Pro at 100°C is 132% of wild-type activity. Catalytic activity of the mutant enzyme has similar response to changes in pH as wild-type enzyme and shows optimal activity at pH 6.0, although the activity is 60% of wild-type activity
R19G/G39E/K71E/S229T
site-directed mutagenesis, the mutant shows altered kinetics and temperature profile
R19G/G39E/K71E/S229T
mutant enzyme shows a higher activity than wild-type enzyme over a broad range of temperatures, the thermostability of the mutant enzymes is less compared to wild type. At 35°C, 70°C and 100°C the mutant exhibits higher Vmax and kcat values than wild-type prolidase for Met-Pro. kcat/Km for Met-Pro is 1.2fold higher than wild-type value at 35°C, kcat/Km for Met -Pro is 1.8fold higher than wild-type value at 70°C, kcat/Km for Met-Pro is 2.5fold higher than wild-type value at 100°C. Relative specific activity towards Met-Pro at 100°C is 143% of wild-type activity. Relative specific activity towards Leu-Pro at 100°C is 79% of wild-type activity. Relative specific activity towards Phe-Pro at 100°C is 122% of wild-type activity. Relative specific activity towards Ala-Pro at 100°C is 38% of wild-type activity. Relative specific activity towards Gly-Pro at 100°C is 10% of wild-type activity. Relative specific activity towards Arg-Pro at 100°C is 112% of wild-type activity
additional information
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construction and expression of leucine zipper mutants and active site mutants, the former show no remaining activity, while the latter are not catalytically active but are still able to dimerize
additional information
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complete map of the known PEPD mutant alleles causing prolidase deficiency, which is a rare recessive disorder characterized by severe skin lesions, single amino acid substitutions, exon splicing, deletions and a duplication are described as causative for the disease and are mainly located at highly conserved amino acids in the sequence of prolidase, genotype-phenotype correlation, clinical phenotype, overview
additional information
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enzyme decficiency leads to a rare autosomal recessive disease, characterized by a wide range of clinical outcomes, including severe skin lesions, mental retardation, and infections of the respiratory tract, genotype/phenotype relationship, overview
additional information
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identification of 17 mutations involved in prolidase deficiency, a rare, pan-ethnic, autosomal recessive disease with a broad phenotypic spectrum. Phenotypes of 20 prolidase deficient patients of Arab Moslem and Druze origin from 10 kindreds residing in northern Israel, overview
additional information
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the use of Pyrococcus furiosus prolidase for organophosphorus nerve agent decontamination is restricted by the fact that this enzyme displays a narrow functional temperature range. Like many other enzymes isolated from hyperthermophiles, Pyrococcus furiosus prolidase has only 50% activity at 80°C and displays little activity at temperatures below 50°C. Therefore a random-mutated Pyrococcus furiosus prolidase gene library is constructed and screened for production of mutants with increased activity at room temperature while maintaining thermostability. The mutant enzyme shows increased activity over the pH range of 57. At pH 5.0, the mutant activity is 1.6fold higher than wild-type activity, and at pH 7.0, it is 1.2fold higher than wild type
additional information
the use of Pyrococcus furiosus prolidase for organophosphorus nerve agent decontamination is restricted by the fact that this enzyme displays a narrow functional temperature range. Like many other enzymes isolated from hyperthermophiles, Pyrococcus furiosus prolidase has only 50% activity at 80°C and displays little activity at temperatures below 50°C. Therefore a random-mutated Pyrococcus furiosus prolidase gene library is constructed and screened for production of mutants with increased activity at room temperature while maintaining thermostability. The mutant enzyme shows increased activity over the pH range of 57. At pH 5.0, the mutant activity is 1.6fold higher than wild-type activity, and at pH 7.0, it is 1.2fold higher than wild type
additional information
randomly mutated enzymes are prepared Tt obtain a better enzyme for organophosphorus nerve agent decontamination and to investigate the structural factors that may influence protein thermostability and thermoactivity
additional information
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randomly mutated enzymes are prepared Tt obtain a better enzyme for organophosphorus nerve agent decontamination and to investigate the structural factors that may influence protein thermostability and thermoactivity
additional information
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randomly mutated enzymes are prepared Tt obtain a better enzyme for organophosphorus nerve agent decontamination and to investigate the structural factors that may influence protein thermostability and thermoactivity
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