Literature summary for 3.5.1.2 extracted from

Yano, S.; Kamemura, A.; Yoshimune, K.; Moriguchi, M.; Yamamoto, S.; Tachiki, T.; Wakayama, M.
Analysis of essential amino acid residues for catalytic activity of glutaminase from Micrococcus luteus K-3 (2006), J. Biosci. Bioeng., 102, 362-364.

Search for more literature for 3.5.1.2

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Micrococcus luteus

Protein Variants

Protein Variants	Comment	Organism
E160D	inactive mutant enzyme	Micrococcus luteus
E160D	mutant enzyme with largely decreased catalytic activity, kcat/Km is 1167fold lower than wild-type value	Micrococcus luteus
K67E	inactive mutant enzyme	Micrococcus luteus
S64A	inactive mutant enzyme	Micrococcus luteus
Y191F	kcat/Km is 39fold lower than wild-type value	Micrococcus luteus
Y191T	kcat/Km is 67742fold lower than wild-type value	Micrococcus luteus

Inhibitors

Inhibitors	Comment	Organism	Structure
6-diazo-5-oxo-L-norleucine	-	Micrococcus luteus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
6.2	-	L-glutamine	mutant enzyme E160D	Micrococcus luteus
6.6	-	L-glutamine	wild-type enzyme	Micrococcus luteus
11	-	L-glutamine	mutant enzyme Y191F	Micrococcus luteus
460	-	L-glutamine	mutant enzyme Y191T	Micrococcus luteus

Organism

Organism	UniProt	Comment	Textmining
Micrococcus luteus	-	-	-
Micrococcus luteus K-3	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-glutamine + H2O	-	Micrococcus luteus	L-glutamate + NH3	-	?
L-glutamine + H2O	-	Micrococcus luteus K-3	L-glutamate + NH3	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.96	-	L-glutamine	mutant enzyme E160D	Micrococcus luteus
1.4	-	L-glutamine	mutant enzyme Y191T	Micrococcus luteus
57	-	L-glutamine	mutant enzyme Y191F	Micrococcus luteus
1400	-	L-glutamine	wild-type enzyme	Micrococcus luteus

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Release 2023.1 (January 2023)