Literature summary for 5.3.1.28 extracted from

Taylor, P.L.; Blakely, K.M.; de Leon, G.P.; Walker, J.R.; McArthur, F.; Evdokimova, E.; Zhang, K.; Valvano, M.A.; Wright, G.D.; Junop, M.S.
Structure and function of sedoheptulose-7-phosphate isomerase, a critical enzyme for lipopolysaccharide biosynthesis and a target for antibiotic adjuvants (2008), J. Biol. Chem., 283, 2835-2845.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Pseudomonas aeruginosa

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapor diffusion method, crystal structures of GmhA in apo, substrate, and product-bound forms	Pseudomonas aeruginosa
hanging drop vapor diffusion method, crystal structures of GmhA in apo, substrate, and product-bound forms	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
D169N	inactive	Escherichia coli
D94N	kcat/Km for D-sedoheptulose 7-phosphate is 1.8fold higher than wild-type value	Escherichia coli
E65N	inactive	Escherichia coli
H180Q	inactive	Escherichia coli
H61Q	kcat/Km for D-sedoheptulose 7-phosphate is 2.5fold lower than wild-type value	Escherichia coli
Q172E	inactive	Escherichia coli
R69Q	inactive	Escherichia coli
T120A	inactive	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.5	-	D-sedoheptulose 7-phosphate	pH 8.0, mutant enzyme R69Q	Escherichia coli
0.9	-	D-sedoheptulose 7-phosphate	pH 8.0, wild-type enzyme	Escherichia coli
1.2	-	D-sedoheptulose 7-phosphate	pH 8.0, mutant enzyme H61Q	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
D-sedoheptulose 7-phosphate	Pseudomonas aeruginosa	first committed step in the formation of ADP-heptose	D-glycero-D-manno-heptose 7-phosphate	-	?
D-sedoheptulose 7-phosphate	Escherichia coli	first committed step in the formation of ADP-heptose	D-glycero-D-manno-heptose 7-phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P63224	-	-
Pseudomonas aeruginosa	Q9HVZ0	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Pseudomonas aeruginosa
-	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-sedoheptulose 7-phosphate	first committed step in the formation of ADP-heptose	Pseudomonas aeruginosa	D-glycero-D-manno-heptose 7-phosphate	-	?
D-sedoheptulose 7-phosphate	first committed step in the formation of ADP-heptose	Escherichia coli	D-glycero-D-manno-heptose 7-phosphate	-	?
D-sedoheptulose 7-phosphate	it is postulated that GmhA acts through an enediol-intermediate isomerase mechanism	Pseudomonas aeruginosa	D-glycero-D-manno-heptose 7-phosphate	-	?
D-sedoheptulose 7-phosphate	it is postulated that GmhA acts through an enediol-intermediate isomerase mechanism	Escherichia coli	D-glycero-D-manno-heptose 7-phosphate	-	?

Synonyms

Synonyms	Comment	Organism
sedoheptulose-7-phosphate isomerase	-	Pseudomonas aeruginosa
sedoheptulose-7-phosphate isomerase	-	Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.23	-	D-sedoheptulose 7-phosphate	pH 8.0, mutant enzyme H61Q	Escherichia coli
0.44	-	D-sedoheptulose 7-phosphate	pH 8.0, wild-type enzyme	Escherichia coli
0.45	-	D-sedoheptulose 7-phosphate	pH 8.0, mutant enzyme R69Q	Escherichia coli

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
0.2	-	D-sedoheptulose 7-phosphate	pH 8.0, mutant enzyme H61Q	Escherichia coli
0.5	-	D-sedoheptulose 7-phosphate	pH 8.0, wild-type enzyme	Escherichia coli
0.9	-	D-sedoheptulose 7-phosphate	pH 8.0, mutant enzyme R69Q	Escherichia coli

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Release 2023.1 (January 2023)