Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.5.2.10 extracted from

  • Kaplan, A.; Szabo, L.L.
    Creatinine hydrolase and creatine amidinohydrolase. II. Partial purification and properties (1974), Mol. Cell. Biochem., 3, 17-25.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
azide complete inhibition at the ionic strength of 2 mM Paenarthrobacter ureafaciens
Cu2+ complete inhibition at the ionic strength of 1 mM CuSO4 Paenarthrobacter ureafaciens
cyanide complete inhibition by 1 mM, much less inhibition by both azide and cyanide Paenarthrobacter ureafaciens
Hg2+ complete inhibition at the ionic strength of 0.1 mM HgCl, 20-30% activity restored at 20 mM 2-mercaptoethanol Paenarthrobacter ureafaciens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
125
-
creatinine
-
Paenarthrobacter ureafaciens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
240000
-
gel filtration Paenarthrobacter ureafaciens

Organism

Organism UniProt Comment Textmining
Paenarthrobacter ureafaciens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
heating, precipitation of nucleic acids with streptomycin, ammonium sulfate precipitation, Sephadex gel filtration, and DEAE-cellulose column chromatography Paenarthrobacter ureafaciens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.3
-
-
Paenarthrobacter ureafaciens