Literature summary for 5.3.1.28 extracted from

Harmer, N.J.
The structure of sedoheptulose-7-phosphate isomerase from Burkholderia pseudomallei reveals a zinc binding site at the heart of the active site (2010), J. Mol. Biol., 400, 379-392.

Search for more literature for 5.3.1.28

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli Rosetta (DE3) cells	Burkholderia pseudomallei

Crystallization (Commentary)

Crystallization (Comment)	Organism
untagged enzyme, hanging drop vapor diffusion method, using 0.1 M Na-acetate, pH 4.6, 8% (w/v) PEG 4000	Burkholderia pseudomallei

Protein Variants

Protein Variants	Comment	Organism
D61A	the mutant exhibits about 17fold reduced catalytic efficiency compared to the wild type enzyme	Burkholderia pseudomallei
D98N	inactive	Burkholderia pseudomallei
E68Q	inactive	Burkholderia pseudomallei
H64Q	the mutant exhibits 12fold reduced catalytic efficiency compared to the wild type enzyme	Burkholderia pseudomallei
Q175E	inactive	Burkholderia pseudomallei
T124A	inactive	Burkholderia pseudomallei

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.3	-	D-sedoheptulose 7-phosphate	mutant enzyme D61A, in 20 mM HEPES, pH 8.0, 10 mM MgCl2, 10 mM KCl, at 37°C	Burkholderia pseudomallei
0.4	-	D-sedoheptulose 7-phosphate	wild type enzyme, in 20 mM HEPES, pH 8.0, 10 mM MgCl2, 10 mM KCl, at 37°C	Burkholderia pseudomallei
0.7	-	D-sedoheptulose 7-phosphate	mutant enzyme H64Q, in 20 mM HEPES, pH 8.0, 10 mM MgCl2, 10 mM KCl, at 37°C	Burkholderia pseudomallei

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	the enzyme contains a zinc ion at the heart of its active site, this ion stabilizes the active, closed form of the enzyme and presents coordinating side chains as a potential acid and base to drive catalysis	Burkholderia pseudomallei

Organism

Organism	UniProt	Comment	Textmining
Burkholderia pseudomallei	Q93UJ2	-	-
Burkholderia pseudomallei K96243	Q93UJ2	-	-

Purification (Commentary)

Purification (Comment)	Organism
nickel-agarose column chromatography and Superdex 200 gel filtration	Burkholderia pseudomallei

Source Tissue

Source Tissue	Comment	Organism	Textmining

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-sedoheptulose 7-phosphate	-	Burkholderia pseudomallei	D-glycero-D-manno-heptose 7-phosphate	-	?
D-sedoheptulose 7-phosphate	-	Burkholderia pseudomallei K96243	D-glycero-D-manno-heptose 7-phosphate	-	?

Synonyms

Synonyms	Comment	Organism
GmhA	-	Burkholderia pseudomallei
phosphoheptose isomerase	-	Burkholderia pseudomallei
S7P isomerase	-	Burkholderia pseudomallei

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.02	-	D-sedoheptulose 7-phosphate	mutant enzyme D61A, in 20 mM HEPES, pH 8.0, 10 mM MgCl2, 10 mM KCl, at 37°C	Burkholderia pseudomallei
0.07	-	D-sedoheptulose 7-phosphate	mutant enzyme H64Q, in 20 mM HEPES, pH 8.0, 10 mM MgCl2, 10 mM KCl, at 37°C	Burkholderia pseudomallei
0.5	-	D-sedoheptulose 7-phosphate	wild type enzyme, in 20 mM HEPES, pH 8.0, 10 mM MgCl2, 10 mM KCl, at 37°C	Burkholderia pseudomallei

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
0.07	-	D-sedoheptulose 7-phosphate	mutant enzyme D61A, in 20 mM HEPES, pH 8.0, 10 mM MgCl2, 10 mM KCl, at 37°C	Burkholderia pseudomallei
0.1	-	D-sedoheptulose 7-phosphate	mutant enzyme H64Q, in 20 mM HEPES, pH 8.0, 10 mM MgCl2, 10 mM KCl, at 37°C	Burkholderia pseudomallei
1.2	-	D-sedoheptulose 7-phosphate	wild type enzyme, in 20 mM HEPES, pH 8.0, 10 mM MgCl2, 10 mM KCl, at 37°C	Burkholderia pseudomallei

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Release 2023.1 (January 2023)