Literature summary for 3.5.2.10 extracted from

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 (2004), J. Mol. Biol., 337, 399-416.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Pseudomonas putida

Crystallization (Commentary)

Crystallization (Comment)	Organism
-	Pseudomonas putida
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	Pseudomonas putida

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mn2+	may substitute for Zn2+	Pseudomonas putida
Zn2+	-	Pseudomonas putida

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas putida	P83772	-	-

Purification (Commentary)

Purification (Comment)	Organism
native and Mn2+-activated enzymes purified, Toyopearl HW65C column and DEAE-Toyopearl column	Pseudomonas putida

Reaction

Reaction	Comment	Organism	Reaction ID
creatinine + H2O = creatine	mechanism	Pseudomonas putida	a

Subunits

Subunits	Comment	Organism
hexamer	dimer of trimers, crystallization data	Pseudomonas putida
hexamer	trimer of dimers, Mn2+-activated creatininase-creatine complex, disc-shaped	Pseudomonas putida

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Release 2023.1 (January 2023)