Literature summary for 2.7.2.11 extracted from

Kaino, T.; Tasaka, Y.; Tatehashi, Y.; Takagi, H.
Functional analysis of the C-terminal region of gamma-glutamyl kinase of Saccharomyces cerevisiae (2012), Biosci. Biotechnol. Biochem., 76, 454-461.

Search for more literature for 2.7.2.11

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli as a His-tagged fusion protein	Saccharomyces cerevisiae

Protein Variants

Protein Variants	Comment	Organism
additional information	truncated yeast gamma-glutamyl kinase proteins are engineered from which the C-terminal region is deleted. A complementation test in Escherichia coli and yeast and enzymatic analysis of recombinant proteins reveal that a 67-residue linker sequence between a 255-residue kinase domain and a 106-residue archaeosine transglycosylase (PUA) domain is essential for gamma-glutamyl kinase activity. 67 or more residues of the C-terminal region, not the PUA domain itself, are required for the full enzymatic activity	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
using Ni-NTA chromatography	Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-glutamate	-	Saccharomyces cerevisiae	ADP + L-glutamate 5-phosphate	-	?

Synonyms

Synonyms	Comment	Organism
gamma-glutamyl kinase	-	Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)