Literature summary for 2.7.1.30 extracted from

Yeh, J.I.; Charrier, V.; Paulo, J.; Hou, L.; Darbon, E.; Claiborne, A.; Hol, W.G.; Deutscher, J.
Structures of enterococcal glycerol kinase in the absence and presence of glycerol: correlation of conformation to substrate binding and a mechanism of activation by phosphorylation (2004), Biochemistry, 43, 362-373.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Enterococcus casseliflavus

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystals of native and mutant enzyme with bound glycerol, hanging drop vapor diffusion method	Enterococcus casseliflavus
in complex with glycerol, ADP and the allosteric effector enzyme IIAGlc	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
H232A	lacks the site of activation by phosphorylation, activity similar to unphosphorylated native enzyme	Enterococcus casseliflavus

Inhibitors

Inhibitors	Comment	Organism	Structure
fructose 1,6-bisphosphate	-	Enterococcus casseliflavus
fructose 1,6-bisphosphate	-	Escherichia coli
additional information	regulation of activity by allosteric inhibition through complex formation with enzyme IIAGlc	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + glycerol	Escherichia coli	key enzyme of glycerol metabolism in bacteria, phosphorylation of glycerol prevents diffusion through membrane	ADP + sn-glycerol 3-phosphate	-	?
ATP + glycerol	Enterococcus casseliflavus	key enzyme of glycerol metabolism in bacteria, phosphorylation of glycerol prevents diffusion through membrane	ADP + sn-glycerol 3-phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Enterococcus casseliflavus	-	-	-
Escherichia coli	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	phosphorylation at His232 activates the kinase 10-15-fold	Enterococcus casseliflavus

Purification (Commentary)

Purification (Comment)	Organism
native and mutant enzyme	Enterococcus casseliflavus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + glycerol	-	Escherichia coli	ADP + sn-glycerol 3-phosphate	-	?
ATP + glycerol	-	Enterococcus casseliflavus	ADP + sn-glycerol 3-phosphate	-	?
ATP + glycerol	key enzyme of glycerol metabolism in bacteria, phosphorylation of glycerol prevents diffusion through membrane	Escherichia coli	ADP + sn-glycerol 3-phosphate	-	?
ATP + glycerol	key enzyme of glycerol metabolism in bacteria, phosphorylation of glycerol prevents diffusion through membrane	Enterococcus casseliflavus	ADP + sn-glycerol 3-phosphate	-	?

Subunits

Subunits	Comment	Organism
dimer	crystal structure analysis, probably active state of enzyme	Escherichia coli
tetramer	composed of two dimers, crystal structure analysis	Enterococcus casseliflavus
tetramer	crystal structure analysis, probably inactive state of enzyme	Escherichia coli

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Release 2023.1 (January 2023)