We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
creatininase, creatinine amidohydrolase, creatinine hydrolase,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
creatinine amidohydrolase
-
-
creatinine hydrolase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
creatinine + H2O = creatine
creatinine + H2O = creatine
-
-
-
-
creatinine + H2O = creatine
mechanism
creatinine + H2O = creatine
mechanism
-
creatinine + H2O = creatine
catalytic mechanism: a first water molecule is a hydroxide ion that is bound as a bridge between the two metal ions and attacks the carbonyl carbon of the substrate. A second water molecule is bound to the carboxyl group of Glu122 and functions as a proton donor in catalysis
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.
creatinine 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.
creatinine + H2O
creatine
creatinine + H2O
?
-
creatine metabolism
-
-
?
creatinine + H2O
?
-
-
-
-
?
creatinine + H2O
?
-
-
-
-
?
creatinine + H2O
?
-
-
-
-
?
creatinine + H2O
?
-
-
-
-
?
creatinine + H2O
creatine
-
-
-
r
creatinine + H2O
creatine
-
-
-
-
?
creatinine + H2O
creatine
-
-
-
r
creatinine + H2O
creatine
-
-
-
r
creatinine + H2O
creatine
-
-
-
?
creatinine + H2O
creatine
-
-
-
-
?
creatinine + H2O
creatine
-
-
-
r
creatinine + H2O
creatine
-
-
-
-
r
creatinine + H2O
creatine
-
-
-
?
creatinine + H2O
creatine
-
-
-
-
?
creatinine + H2O
creatine
-
-
-
r
creatinine + H2O
creatine
-
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
creatinine + H2O
creatine
-
-
-
-
?
creatinine + H2O
?
-
creatine metabolism
-
-
?
creatinine + H2O
?
-
-
-
-
?
creatinine + H2O
?
-
-
-
-
?
creatinine + H2O
?
-
-
-
-
?
creatinine + H2O
?
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Zinc
removal of the zinc ions by dialyzing against buffers containing o-phenanthroline results in a partial decrease of 10-30% in activity and zinc content. Wild-type enzyme, purified in the presence of EDTA, shows only half the activity of the wild-type enzyme, the activity is recovered by the addition of ZnCl2 or MnCl2
Mn2+
-
activates
Mn2+
may substitute for Zn2+
Zn2+
-
Zn2+
-
one gatom Zn2+ per mol of subunit monomer
Zn2+
one zinc centre per monomer
Zn2+
-
contains one zinc ion per subunit
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
azide
-
complete inhibition at the ionic strength of 2 mM
cyanide
-
complete inhibition by 1 mM, much less inhibition by both azide and cyanide
ethoxyformic anhydride
-
-
Hg2+
-
complete inhibition at the ionic strength of 0.1 mM HgCl, 20-30% activity restored at 20 mM 2-mercaptoethanol
additional information
-
-
-
Cu2+
-
complete inhibition at the ionic strength of 1 mM CuSO4
EDTA
-
-
EDTA
wild-type enzyme, purified in the presence of EDTA, shows only half the activity of the wild-type enzyme, the activity is recovered by the addition of ZnCl2 or MnCl2
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.
Kidney Failure, Chronic
Induction of creatininase activity in chronic renal failure: timing of creatinine degradation and effect of antibiotics.
Rhabdomyolysis
[Acute ischemia of the leg in a drug addict]
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
additional information
-
steady-state Michaelis-Menten kinetics
-
0.17
creatinine
-
pH 7.5, 30°C
4.1
creatinine
-
pH 7.4, 20°C
44
creatinine
wild-type, presence of Zn2+, pH not specified in the publication, temperature not specified in the publication
56
creatinine
mutant E122Q, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
77
creatinine
wild-type, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
90
creatinine
mutant W174F, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
150
creatinine
wild-type, presence of EDTA, semi-apo-enzyme, pH not specified in the publication, temperature not specified in the publication
160
creatinine
mutant Y121A, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
220
creatinine
mutant E122Q, presence of Zn2+, pH not specified in the publication, temperature not specified in the publication
350
creatinine
mutant W154F, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.5
creatinine
mutant E122Q, presence of Zn2+, pH not specified in the publication, temperature not specified in the publication
11
creatinine
mutant E122Q, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
18
creatinine
mutant W154F, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
86
creatinine
mutant Y121A, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
222
creatinine
wild-type, presence of EDTA, semi-apo-enzyme, pH not specified in the publication, temperature not specified in the publication
252
creatinine
wild-type, presence of Zn2+, pH not specified in the publication, temperature not specified in the publication
688
creatinine
mutant W174F, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
1340
creatinine
wild-type, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.008
creatinine
mutant E122Q, presence of Zn2+, pH not specified in the publication, temperature not specified in the publication
0.051
creatinine
mutant W154F, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
0.2
creatinine
mutant E122Q, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
0.54
creatinine
mutant Y121A, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
1.48
creatinine
wild-type, presence of EDTA, semi-apo-enzyme, pH not specified in the publication, temperature not specified in the publication
5.73
creatinine
wild-type, presence of Zn2+, pH not specified in the publication, temperature not specified in the publication
7.64
creatinine
mutant W174F, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
17.4
creatinine
wild-type, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.13
mutant E122Q, presence of Zn2+, pH not specified in the publication, temperature not specified in the publication
13.9
mutant E122Q, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
140
mutant Y121A, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
1560
wild-type, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
178
wild-type, presence of EDTA, semi-apo-enzyme, pH not specified in the publication, temperature not specified in the publication
370
wild-type, presence of Zn2+, pH not specified in the publication, temperature not specified in the publication
4.9
mutant W154F, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
740
mutant W174F, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
additional information
-
by Escherichia coli transformants pCRN741 without and with IPTG 0.678 U per ml
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7.7
-
immobilized coupled enzyme system
8.5
-
immobilized coupled enzyme system
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7 - 8
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
25
-
immobilized coupled enzyme system
45
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
Sigma, Cat. No.C-7399, lot 20 Ho349
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
SwissProt
brenda
-
-
-
brenda
-
SwissProt
brenda
NTU-8 and its creatininase producing mutant RS65
-
-
brenda
var. naraensis, strain C-83
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
-
brenda
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.
173000
-
dynamic light scattering
175000
-
ultracentrifugal analysis
23000
-
8 * 23000, SDS-PAGE
28399
-
6 * 28399, calculated from amino acid sequence
28400
-
6 * 28400, MALDI-TOF mass spectrometry
28440
-
recombinant polypeptide deduced from the nucleotide sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dimer
-
dimer with a molecular weight of 175000
hexamer
dimer of trimers, crystallization data
hexamer
trimer of dimers, crystallization data
hexamer
trimer of dimers, Mn2+-activated creatininase-creatine complex, disc-shaped
homohexamer
-
6 * 28399, calculated from amino acid sequence
homohexamer
-
6 * 28400, MALDI-TOF mass spectrometry
octamer
-
8 * 23000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
glycoprotein
-
3.5% glucose
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
crystal structure of the enzyme complexed with a 1-methylguanidine. All subunits in the complex exist as the closed form. X-ray crystallographic study and the atomic absorption spectrometry analysis of the E122Q mutant-substrate complex reveal that the drastic decrease of the activity of the E122Q is caused by the loss of one Zn ion at the Metal1 site and a critical function of Glu122
crystal structures of the native and the Mn2+-activated enzyme determined by a difference Fourier method, crystal structure of Mn2+-activated enzyme determined by the single isomorphous replacement method
hanging drop vapour diffusion method with 1.5 M lithium sulfate in 0.1 M Na-HEPES pH 7.5
-
sitting drop vapour diffusion method with 22% ethanol, 20% PEG 8000, and 0.1 M MOPS pH 7.5
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
E122Q
almost complete loss of activity
E183Q
complete loss of activity
H178A
complete loss of activity
W154A
complete loss of activity
W154F
almost complete loss of activity
W174A
almost complete loss of activity
W174F
about 50% of wild-type activity
Y121A
about 10% of wild-type catalytic efficiency
additional information
-
construction of an electrochemical biosensor for creatinine based on the immobilization of creatininase, creatinase and sarcosine oxidase onto a ferrocene/horseradish peroxidase/gold nanoparticles/multi-walled carbon nanotubes/Teflon composite electrode,method development and evaluation, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
6 - 12
-
for 3 h at 30°C
172079
6 - 9
-
the enzyme tends to precipitate at pH values of under 6.0 and over 9.0 corresponding to the stability range of the enzyme
677306
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
55
-
30 min at pH 7.1, apoenzyme
70
-
30 min at pH 7.1, native enzyme
75
-
30 min, activity still 40%
75
-
30 min, activity still 40%
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
enzyme immobilized have a long-term stability, unused 6 month
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
unstable to photooxidation
-
172079
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4°C, 0.1 M phosphate buffer, pH 7.7, enzymes controlled-pore glass immobilized
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ammonium sulfate fractionation, DEAE Sepharose CL-6B and Sepharose CL-6B column chromatographies, 50% total activity
-
heating, precipitation of nucleic acids with streptomycin, ammonium sulfate precipitation, Sephadex gel filtration, and DEAE-cellulose column chromatography
-
native and Mn2+-activated enzymes purified, Toyopearl HW65C column and DEAE-Toyopearl column
purified by column chromarographies on sarcosine-HM-Sepharose and DEAE-cellulose, and gel filtration on Sephadex G-200
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
cloned, sequenced and expressed in Escherichia coli DH5?, vector pCRN741, creatininase gene consists of 771 bp, encodes 257 amino acids, similarity of RS65 to PS-7 72.8% and Arthrobacter sp. TE1826 43.2%
-
expressed in Escherichia coli
-
expression in Escherichia coli
in Escherichia coli C600 harboring pCNH5-13, Insert contains 780 bp, 259 amino acids
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
wild-type enzyme, purified in the presence of EDTA, shows only half the activity of the wild-type enzyme, the activity is recovered by the addition of ZnCl2 or MnCl2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
diagnostics
-
the immobilized enzyme can be used in a biosensor for determining creatinine in human serum
analysis
-
analysis of serum creatinine concentration
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 30°C, when polarized at 0.4 V versus Ag/AgCl. The electrocatalytic response shows a linear dependence on creatinine concentration ranging from 1 to 800 microM. 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 4°C. The biosensor measures creatinine in the serum of apparently healthy persons
medicine
-
to assess renal function
medicine
-
diagnosis of renal, muscular and thyroid functions
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Tang, T.Y.; Wen, C.J.
Expression of the creatininase gene from Pseudomonas putida RS65 in Escherichia coli
J. Ind. Microbiol.
24
2-6
2000
Alcaligenes sp., Pseudomonas putida
-
brenda
Rikitake, K.; Oka, I.; Ando, M.; Yoshimoto, T.; Tsuru, D.
Creatinine amidohydrolase (creatininase) from Pseudomonas putida. Purification and some properties
J. Biochem.
86
1109-1117
1979
Pseudomonas putida
brenda
Tsuru, D.; Oka, I.; Yoshimoto, T.
Creatinine decomposing enzymes in Pseudomonas putida
Agric. Biol. Chem.
40
1011-1018
1976
Paenarthrobacter ureafaciens, Pseudomonas aeruginosa, Pseudomonas putida
-
brenda
Yamamoto, K.; Oka, M.
Cloning of the creatinine amidohydrolase gene from Pseudomonas sp. PS-7
Biosci. Biotechnol. Biochem.
59
1331-1332
1995
Pseudomonas sp.
brenda
Tabata, M.; Totani, M.
Coimmobilized enzyme columns in determining serum creatinine, creatinase and sarcosine oxidase by flow-injektion analysis and chemiluminescence detection
Anal. Chim. Acta
262
315-321
1992
Pseudomonas sp.
-
brenda
Kaplan, A.; Szabo, L.L.
Creatinine hydrolase and creatine amidinohydrolase. II. Partial purification and properties
Mol. Cell. Biochem.
3
17-25
1974
Paenarthrobacter ureafaciens
brenda
Sakslund, H.; Hammerich, O.
Effects of pH, temperature and reaction products on the performance of an immobilized creatininase-creatinase-sarcosine oxidase enzyme system for creatinine determination
Anal. Chim. Acta
268
331-345
1992
Flavobacterium sp.
-
brenda
Beuth, B.; Niefind, K.; Schomburg, D.
Crystal structure of creatininase from Pseudomonas putida: a novel fold and a case of convergent evolution
J. Mol. Biol.
332
287-301
2003
Pseudomonas putida (P83772), Pseudomonas putida
brenda
Yoshimoto, T.; Tanaka, N.; Kanada, N.; Inoue, T.; Nakajima, Y.; Haratake, M.; Nakamura, K.T.; Xu, Y.; Ito, K.
Crystal structures of creatininase reveal the substrate binding site and provide an insight into the catalytic mechanism
J. Mol. Biol.
337
399-416
2004
Pseudomonas putida (P83772), Pseudomonas putida
brenda
Beuth, B.; Niefind, K.; Schomburg, D.
Crystallization and preliminary crystallographic analysis of creatininase from Pseudomonas putida
Acta Crystallogr. Sect. D
58
1356-1358
2002
Pseudomonas putida
brenda
Ito, K.; Kanada, N.; Inoue, T.; Furukawa, K.; Yamashita, K.; Tanaka, N.; Nakamura, K.T.; Nishiya, Y.; Sogabe, A.; Yoshimoto, T.
Preliminary crystallographic studies of the creatinine amidohydrolase from Pseudomonas putida
Acta Crystallogr. Sect. D
58
2180-2181
2002
Pseudomonas putida
brenda
Yamashita, K.; Nakajima, Y.; Matsushita, H.; Nishiya, Y.; Yamazawa, R.; Wu, Y.F.; Matsubara, F.; Oyama, H.; Ito, K.; Yoshimoto, T.
Substitution of Glu122 by glutamine revealed the function of the second water molecule as a proton donor in the binuclear metal enzyme creatininase
J. Mol. Biol.
396
1081-1096
2010
Pseudomonas putida (P83772)
brenda
Yadav, S.; Devi, R.; Bhar, P.; Singhla, S.; Pundir, C.S.
Immobilization of creatininase, creatinase and sarcosine oxidase on iron oxide nanoparticles/chitosan-g-polyaniline modified Pt electrode for detection of creatinine
Enzyme Microb. Technol.
50
247-254
2012
Pseudomonas sp.
brenda
Serafin, V.; Hernandez, P.; Agui, L.; Yanez-Sedeno, P.; Pingarron, J.
Electrochemical biosensor for creatinine based on the immobilization of creatininase, creatinase and sarcosine oxidase onto a ferrocene/horseradish peroxidase/gold nanoparticles/multi-walled carbon nanotubes/Teflon composite electrode
Electrochim. Acta
97
175-183
2013
Homo sapiens
-
brenda
Select items on the left to see more content.
html completed