Literature summary 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.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
3.5.2.10	expression in Escherichia coli	Pseudomonas putida

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
3.5.2.10	-	Pseudomonas putida
3.5.2.10	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

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

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.5.2.10	Pseudomonas putida	P83772	-	-

Purification (Commentary)

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

Reaction

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

Subunits

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

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Release 2023.1 (January 2023)