Information on EC 3.5.3.3 - creatinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.5.3.3
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RECOMMENDED NAME
GeneOntology No.
creatinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
creatine + H2O = sarcosine + urea
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of linear amidines
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
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creatinine degradation I
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Glycine, serine and threonine metabolism
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Metabolic pathways
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creatinine degradation
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SYSTEMATIC NAME
IUBMB Comments
creatine amidinohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
37340-58-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subsp. denitrificans J9
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Manually annotated by BRENDA team
CRH-104D
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-
Manually annotated by BRENDA team
AK-2
-
-
Manually annotated by BRENDA team
J5 and J11
-
-
Manually annotated by BRENDA team
B-068
-
-
Manually annotated by BRENDA team
B-068
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
NTU-8
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-
Manually annotated by BRENDA team
C-83
-
-
Manually annotated by BRENDA team
H21 AKU876
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
creatine + H2O
?
show the reaction diagram
creatine + H2O
sarcosine + urea
show the reaction diagram
pseudothiohydantoic acid + H2O
?
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
creatine + H2O
?
show the reaction diagram
creatine + H2O
sarcosine + urea
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
1 mM, 104% of initial activity
Fe2+
-
FeSO4, activates
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
-
complete inactivation at 1 mM
CaCl2
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1 mM, 32% inhibition
carbamoyl sarcosine
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Co2+
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50% inhibition at 1 mM
CoCl2
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1 mM, 71% inhibition
DFP
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1 mM, 30% inhibition
diethyldithiocarbamate
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EDTA
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2 mM, 10% inhibition
Fe3+
1 mM, 2.2% residual activity
FeCl3
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1 mM, 71% inhibition
MgSO4
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1 mM, 31% inhibition
N-bromosuccinimide
Pb-Acetate
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1 mM, 15% inhibition
S-(2-aminoethyl)-isothiuronium bromide
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sarcosine
sodium dodecylsulfate
5 g/l, no residual activity
succinamic acid
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succinic acid
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Tween20
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strong inhibition at 1 mM
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N3-
1 mM, 104% of initial activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.034 - 53.2
Creatine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.246
Creatine
Pseudomonas putida
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0014
crude enzyme, at pH 7.5 and 37°C
0.0203
after 14.1fold purification, at pH 7.5 and 37°C
6.1
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purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7
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immobilized creatininase-creatinase-sarcosine oxidase enzyme system
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9.5
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6.5 - 9.5
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pH 6.5: about 70% of maximal activity, pH 9.5: about 30% of maximal activity
6.5 - 8
60% activity at pH 6.5 and 8.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
immobilized creatininase-creatinase-sarcosine oxidase enzyme system
33
optimum temperature range calculated between 32 and 34°C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 50
26 - 43
optimum temperature range calculated between 32 and 34°C due to the increased kinetic energy of the reacting molecules, current of the bioelectrode measured at different temperatures ranging from 26 to 43°C in the presence of creatine 150 microM and a phosphate buffer (50 mM, pH 7.0)
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
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2 * 43000, SDS-PAGE
45691
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x * 45691, calculation from nucleotide sequence
46500
MALDI-TOF
47000
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2 * 47000, SDS-PAGE
48000
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x * 48000, SDS-PAGE
51000
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gel filtration
92000
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gel filtration
94000
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meniscus depletion method
180000
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additional information
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amino acid sequence comparison suggests that the structure of E. coli methionine aminopeptidase and the C-terminal domain of Pseudomonas putida creatinase are related
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
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1 * 51000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion followed by macroseeding using PEG 6000 as a precipitant
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
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stable
288986
5.5 - 9.5
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purified enzyme, stable
689820
6 - 11
the enzyme is stable in the range of pH 6.0 to 11.0 for 6 h incubation
733140
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 50
-
purified enzyme, stable
26 - 43
thermal stability of the bioelectrode studied by measuring the current at different temperatures ranging from 26 to 43°C in the presence of creatine at 150 microM and a phosphate buffer (50 mM, pH 7.0)
30
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irreversible loss of some of the activity above
40 - 50
the enzyme is stable below 40°C but completely loses its activity after 30 min preincubation at 50°C
40
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stable
55
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15 min, completely destroyed
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of 0.2 M NaCl stabilizes against the solubilizing effect of urea. Methylurea has higher denaturing capacity than urea. At glycerol concentrations up to 20% creatinase is in its native state
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enzyme shows anomalously low intrinsic stability and is inaccessible to reconstitution after preceding deactivation, denaturation and dissociation
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stability of creatine amidinohydrolase-containing polyurethane hydrogels stored in buffer at 37°C decreases after 1 week, PEGylation of creatine-amidinohydrolase leads to decrease of half-life when stored in buffer at 37°C
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stabilized by addition of nonionic detergents with a hydrophile-lipophile balance value of more than 14, chelating agents, or preservatives
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unused enzyme in the immobilized creatininase-creatinase-sarcosine oxidase enzyme system maintains activity for at least 6 months. Activity remains unchanged after heavy daily use of 20-30 days
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upon increasing the concentration of the enzyme from 0.003 to 0.024 mg/ml the apparent concentration of guanidinium chloride where 50% denaturation are observed shifts from 0.35 to 0.44 M
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Triton X-100
Tween 20
Tween 80
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, HiPrep column chromatography, and Superdex 200 gel filtration
native enzyme 10.17fold to homogeneity by anion exchange chromatography, hydrophobic interaction chromatography, and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression and export by Escherichia coli using the chitinase signal sequence of Aeromonas hydrophila. The amount of the fusion enzyme is about 50% exported into the periplasmic space of Escherichia coli
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expression in Escherichia coli
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phylogenetic tree, overview
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A109V
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enhanced thermal stability compared to wild-type enzyme
A109V/V355M
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enhanced thermal stability compared to wild-type enzyme, contributions of single point mutations to the thermal stability are additive
A109V/V355M/V182I
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enhanced thermal stability compared to wild-type enzyme, contributions of single point mutations to the thermal stability are additive
V182I
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no thermal stabilization
V355M
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enhanced thermal stability compared to wild-type enzyme
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme shows anomalously low intrinsic stability and is inaccessible to reconstitution after preceding deactivation, denaturation and dissociation
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
medicine
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