Information on EC 3.5.3.3 - creatinase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
3.5.3.3
-
RECOMMENDED NAME
GeneOntology No.
creatinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
creatine + H2O = sarcosine + urea
show the reaction diagram
mechanism
-
creatine + H2O = sarcosine + urea
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of linear amidines
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
creatinine degradation I
-
Glycine, serine and threonine metabolism
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
creatine amidinohydrolase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CAH
Q7SIB5
-
CAH
Actinobacillus sp. CRH-211
Q7SIB5
-
-
Creatine amidinohydrolase
-
-
-
-
Creatine amidinohydrolase
-
-
Creatine amidinohydrolase
Q7SIB5
-
Creatine amidinohydrolase
Actinobacillus sp. CRH-211
-, Q7SIB5
-
-
CAS REGISTRY NUMBER
COMMENTARY
37340-58-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
subsp. denitrificans J9
-
-
Manually annotated by BRENDA team
CRH-104D
-
-
Manually annotated by BRENDA team
Acinetobacter sp. CRH-104D
CRH-104D
-
-
Manually annotated by BRENDA team
strain CRH-211
-
-
Manually annotated by BRENDA team
strain CRH-211
SwissProt
Manually annotated by BRENDA team
Actinobacillus sp. CRH-211
strain CRH-211
-
-
Manually annotated by BRENDA team
Actinobacillus sp. CRH-211
strain CRH-211
SwissProt
Manually annotated by BRENDA team
Alcaligenes sp. AK-2
AK-2
-
-
Manually annotated by BRENDA team
J5 and J11
-
-
Manually annotated by BRENDA team
B-068
-
-
Manually annotated by BRENDA team
Bacillus sp. B-068
B-068
-
-
Manually annotated by BRENDA team
U-188, ATCC 31200
-
-
Manually annotated by BRENDA team
var. naraensis C-83
-
-
Manually annotated by BRENDA team
wild-type enzyme and mutant enzymes A109V, V355M, V181I, A109V/V355M, A109V/V355M/V182I
-
-
Manually annotated by BRENDA team
Pseudomonas putida NTU-8
NTU-8
-
-
Manually annotated by BRENDA team
H21 AKU876
-
-
Manually annotated by BRENDA team
Pseudomonas sp. C-83
C-83
-
-
Manually annotated by BRENDA team
Pseudomonas sp. H21 AKU876
H21 AKU876
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
Q7SIB5
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
A7LCN3
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
Q7SIB5
biomatrix fabricated to investigate immobilization of creatine amidinohydrolase
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
Pseudomonas sp. C-83
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
Actinobacillus sp. CRH-211
-
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
Actinobacillus sp. CRH-211
Q7SIB5
-, biomatrix fabricated to investigate immobilization of creatine amidinohydrolase
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
Pseudomonas putida NTU-8
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
Bacillus sp. B-068
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
Alcaligenes sp. AK-2
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
Arthrobacter sp. J5 J11
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
Acinetobacter sp. CRH-104D
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
Pseudomonas sp. H21 AKU876
-
-
-
?
creatine + H2O
?
show the reaction diagram
-
degradation of creatine, inducible enzyme
-
-
-
pseudothiohydantoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
creatine + H2O
sarcosine + urea
show the reaction diagram
Q7SIB5
-
-
-
?
creatine + H2O
sarcosine + urea
show the reaction diagram
-
-
-
-
?
creatine + H2O
?
show the reaction diagram
-
degradation of creatine, inducible enzyme
-
-
-
creatine + H2O
sarcosine + urea
show the reaction diagram
Actinobacillus sp. CRH-211
Q7SIB5
-
-
-
?
creatine + H2O
?
show the reaction diagram
Arthrobacter sp. J5 J11
-
degradation of creatine, inducible enzyme
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
A7LCN3
1 mM, 104% of initial activity
Fe2+
-
FeSO4, activates
additional information
-
not a metal-dependent enzyme
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Ag+
-
complete inactivation at 1 mM
CaCl2
-
1 mM, 32% inhibition
carbamoyl sarcosine
-
-
Co2+
-
50% inhibition at 1 mM
CoCl2
-
1 mM, 71% inhibition
Cu2+
-
1 mM CuSO4, complete inhibition
Cu2+
-
complete inactivation at 1 mM
Cu2+
A7LCN3
1 mM, no residual activity
DFP
-
1 mM, 30% inhibition
diethyldithiocarbamate
-
-
EDTA
-
2 mM, 10% inhibition
Fe3+
A7LCN3
1 mM, 2.2% residual activity
-
FeCl3
-
1 mM, 71% inhibition
Hg2+
-
1 mM HgCl2, complete inhibition
Hg2+
-
complete inactivation at 1 mM
Hg2+
A7LCN3
1 mM, 9.8% residual activity
N-bromosuccinimide
-
-
N-bromosuccinimide
-
1 mM, 30% inhibition
Pb-Acetate
-
1 mM, 15% inhibition
PCMB
-
0.5 mM, complete inhibition
S-(2-aminoethyl)-isothiuronium bromide
-
-
sodium dodecylsulfate
A7LCN3
5 g/l, no residual activity
succinamic acid
-
-
succinic acid
-
-
Tween20
-
strong inhibition at 1 mM
Zn2+
-
1 mM ZnCl2, complete inhibition
Zn2+
-
40% inhibition at 1 mM
Zn2+
A7LCN3
1 mM, 44% residual activity
MgSO4
-
1 mM, 31% inhibition
additional information
-
NaN3, and chelating agents EDTA and 1,10-phenanthroline do not inhibit the activity at the concentration of 20 mM, no inhibition by Tween80 and SDS, and by Ca2+, Pb2+, Ba2+, Fe2+, Fe3+, Mg2+, Cr2+, Mn2+, and Li+
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
N3-
A7LCN3
1 mM, 104% of initial activity
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.034
-
Creatine
-
pH 7.5, 37C
0.5
-
Creatine
Q7SIB5
parameter calculated for the bioelectrode, depends on the electrode material and the enzyme immobilization process, indicates that nanocomposite matrix has a high affinity to immobilize CAH enzyme, the small Km value indicates a high enzyme affinity to the nanocomposite matrix over the electrode surface, attributed to the advantageous nanoporous surface for the enzyme immobilization that can favor conformational changes of the enzyme, also attributed to high surface-to-volume ratio, which can help to effectively immobilize the enzyme onto the nanocomposite
1.33
-
Creatine
-
-
12.5
-
Creatine
-
mutant A109V
13.3
-
Creatine
-
wild type enzyme
13.9
-
Creatine
-
mutant V355M
14.7
-
Creatine
-
mutant V182I
15.6
-
Creatine
-
mutant A109V/V355M/V182I
16.1
-
Creatine
-
mutant A109V/V355M
17.2
-
Creatine
-
-
20
-
Creatine
-
-
46
-
Creatine
A7LCN3
pH 7.0, 37C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.246
-
Creatine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.1
-
-
purified enzyme
124.4
-
A7LCN3
pH 7.0, 37C
additional information
-
-
measurement of creatinine in a coupled assay with creatininase and sarcosine oxidase, overview
additional information
-
Q7SIB5
biomatrix fabricated to investigate immobilization of creatine amidinohydrolase, characterized with Fourier transform infrared spectroscopy (FTIR), scanning electron microscopy (SEM) and cyclic voltammetry (CV), enzyme affinity to the nanocomposite matrix estimated using the Hanes plot, photometric study to calculate the apparent enzyme activity, influence of various parameters on enzyme activity within the matrix analyzed including pH, temperature, time
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
Q7SIB5
optimum of enzyme activity attributed to the potential positive influence of the dehydrated chitosan on the enzyme activity, suggests that chitosan-SiO2-multiwall carbon nanotubes nanocomposite matrix is suitable for enzyme applications at neutral condition
7.7
-
-
immobilized creatininase-creatinase-sarcosine oxidase enzyme system
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8
Q7SIB5
electrode matrix suitable for enzyme applications at neutral condition
6.5
9.5
-
pH 6.5: about 70% of maximal activity, pH 9.5: about 30% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
immobilized creatininase-creatinase-sarcosine oxidase enzyme system
33
-
Q7SIB5
optimum temperature range calculated between 32 and 34C
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
26
43
Q7SIB5
optimum temperature range calculated between 32 and 34C due to the increased kinetic energy of the reacting molecules, current of the bioelectrode measured at different temperatures ranging from 26 to 43C in the presence of creatine 150 microM and a phosphate buffer (50 mM, pH 7.0)
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
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
-
Manually annotated by BRENDA team
Pseudomonas putida NTU-8
-
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
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
46500
-
Q7SIB5
MALDI-TOF
51000
-
-
gel filtration
90000
-
A7LCN3
PAGE
92000
-
-
gel filtration
94000
-
-
meniscus depletion method
100000
-
-
-
180000
-
-
-
additional information
-
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 45691, calculation from nucleotide sequence
?
-
x * 48000, SDS-PAGE
?
Pseudomonas putida NTU-8
-
x * 45691, calculation from nucleotide sequence
-
dimer
-
2 * 43000, SDS-PAGE
dimer
-
2 * 47000, SDS-PAGE
dimer
-
crystallization data
dimer
A7LCN3
2 * 46400, SDS-PAGE
homodimer
-
-
homodimer
Actinobacillus sp. CRH-211
-
-
-
monomer
-
1 * 51000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop vapor diffusion followed by macroseeding using PEG 6000 as a precipitant
Q7SIB5
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
9
-
stable
5.5
9.5
-
purified enzyme, stable
6
8
-
stable
6
8
-
37C, 24 h stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
50
-
purified enzyme, stable
26
43
Q7SIB5
thermal stability of the bioelectrode studied by measuring the current at different temperatures ranging from 26 to 43C in the presence of creatine at 150 microM and a phosphate buffer (50 mM, pH 7.0)
30
-
-
irreversible loss of some of the activity above
40
-
-
stable
45
-
-
pH 7.4, 50% loss of activity after 30 min
45
-
A7LCN3
stable below
55
-
-
15 min, completely destroyed
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
stability of creatine amidinohydrolase-containing polyurethane hydrogels stored in buffer at 37C decreases after 1 week, PEGylation of creatine-amidinohydrolase leads to decrease of half-life when stored in buffer at 37C
-
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
-
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
-
enzyme shows anomalously low intrinsic stability and is inaccessible to reconstitution after preceding deactivation, denaturation and dissociation
-
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
-
stabilized by addition of nonionic detergents with a hydrophile-lipophile balance value of more than 14, chelating agents, or preservatives
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
native enzyme 10.17fold to homogeneity by anion exchange chromatography, hydrophobic interaction chromatography, and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
phylogenetic tree, overview
-
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
-
expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A109V
-
enhanced thermal stability compared to wild-type enzyme
A109V/V355M
-
enhanced thermal stability compared to wild-type enzyme, contributions of single point mutations to the thermal stability are additive
A109V/V355M/V182I
-
enhanced thermal stability compared to wild-type enzyme, contributions of single point mutations to the thermal stability are additive
V182I
-
no thermal stabilization
V355M
-
enhanced thermal stability compared to wild-type enzyme
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
enzyme shows anomalously low intrinsic stability and is inaccessible to reconstitution after preceding deactivation, denaturation and dissociation
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
Q7SIB5
biomatrix fabricated to investigate immobilization of creatine amidinohydrolase
medicine
-
creatinine determination in biological fluids
medicine
Q7SIB5
creatinase may play a role in the disease process caused by Actinobacillus
analysis
Actinobacillus sp. CRH-211
-
biomatrix fabricated to investigate immobilization of creatine amidinohydrolase
-
medicine
Actinobacillus sp. CRH-211
-
creatinine determination in biological fluids
-
analysis
-
construction of a biosensor by co-immobilization of creatininase, creatinase, and sarcosine oxidase onto iron oxide nanoparticles/chitosangraft-polyaniline, Fe3O4-NPs/CHIT-g-PANI, composite film electrodeposited on surface of Pt electrode through glutaraldehyde coupling. The creatinine biosensor uses enzymes/Fe3O4-NPs/CHIT-g-PANI/Pt electrode as working electrode, Ag/AgCl as reference electrode and Pt wire as auxiliary electrode. The biosensor exhibits an optimum response within 2 s at pH 7.5 and 30C, when polarized at 0.4 V versus Ag/AgCl. The electrocatalytic response shows a linear dependence on creatinine concentration ranging from 1 to 800 M. The sensitivity of the biosensor is 3.9 microA per microM and cm2, with a detection limit of 1 microM. The biosensor shows only 10% loss in its initial response after 120 uses over 200 days, when stored at 4C. The biosensor measures creatinine in the serum of apparently healthy persons