ChemicalBook--->CAS DataBase List--->9025-13-2

9025-13-2

9025-13-2 Structure

9025-13-2 Structure
IdentificationBack Directory
[Name]

EC 3.5.2.10
[CAS]

9025-13-2
[Synonyms]

CAH
C:C&B12
EC 3.5.2.10
CREATININASE
Einecs 232-786-8
CREATININE HYDROLASE
Creatine Amidinohydroase
CREATININE AMIDOHYDROLASE
CREATININE AMINOHYDROLASE
Creatinine amide hydrolase
Creatininase aMidohydrolase
CAH/Creatininase aMidohydrolase
Creatininase from microorganisms
creatininase from pseudomonas sp.
Native microorganisms Creatininase
creatininase from pseudomonas species
Creatininase/Creatinine Amidohydrolase
CREATININASE, PSEUDOMONAS SPECIES, REC
Creatininase from E. coli, Recombinant
Creatininase amidohydrolase USP/EP/BP
Creatininase from Flavobacterium sp.
creatininase from ochrobactrum anthropi
CREATININASE FROM PSEUDOMONAS SP., ~80 U /MG
Creatininase ex. Recombinant E.Coli, 500U/mg
Native Pseudomonas sp. Creatinine amidohydrolase
Creatininase/Creatinine Amidohydrolase, 160 KDa (SDS-PAGE)
[EINECS(EC#)]

232-786-8
[MDL Number]

MFCD00130877
Chemical PropertiesBack Directory
[storage temp. ]

2-8°C
[form ]

lyophilized powder
[color ]

White to off-white
[Specific Activity]

100-300units/mg protein
[EPA Substance Registry System]

Creatininase (9025-13-2)
Safety DataBack Directory
[Symbol(GHS) ]


GHS08
[Signal word ]

Danger
[Hazard statements ]

H334
[Precautionary statements ]

P261-P284-P501
[Safety Statements ]

22-24/25
[WGK Germany ]

3
[F ]

10-21
[TSCA ]

TSCA listed
[Storage Class]

11 - Combustible Solids
[Hazard Classifications]

Resp. Sens. 1
Hazard InformationBack Directory
[Uses]

This enzyme is useful for enzymatic determination of creatinine when coupled with creatine amidinohydrolase, sarcosine dehydrogenase or sarcosine oxidase and formaldehyde dehydrogenase in clinical analysis.
[Biochem/physiol Actions]

Creatininase from Pseudomonas sp. is a homohexameric enzyme with a molecular mass of 28.4 kDa per subunit. It is a cyclic amidohydrolase catalysing the reversible conversion of creatinine to creatine. Each monomer contains a binuclear zinc centre near the C termini of the β-strands and the N termini of the main α-helices. These zinc ions indicate the location of the active site.
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