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Literature summary extracted from
- 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.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.3.1.28 | expression in Escherichia coli | Pseudomonas aeruginosa |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 5.3.1.28 | hanging drop vapor diffusion method, crystal structures of GmhA in apo, substrate, and product-bound forms | Pseudomonas aeruginosa |
| 5.3.1.28 | hanging drop vapor diffusion method, crystal structures of GmhA in apo, substrate, and product-bound forms | Escherichia coli |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 5.3.1.28 | D169N | inactive | Escherichia coli |
| 5.3.1.28 | D94N | kcat/Km for D-sedoheptulose 7-phosphate is 1.8fold higher than wild-type value | Escherichia coli |
| 5.3.1.28 | E65N | inactive | Escherichia coli |
| 5.3.1.28 | H180Q | inactive | Escherichia coli |
| 5.3.1.28 | H61Q | kcat/Km for D-sedoheptulose 7-phosphate is 2.5fold lower than wild-type value | Escherichia coli |
| 5.3.1.28 | Q172E | inactive | Escherichia coli |
| 5.3.1.28 | R69Q | inactive | Escherichia coli |
| 5.3.1.28 | T120A | inactive | Escherichia coli |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.3.1.28 | 0.5 | - |
D-sedoheptulose 7-phosphate | pH 8.0, mutant enzyme R69Q | Escherichia coli |  |
| 5.3.1.28 | 0.9 | - |
D-sedoheptulose 7-phosphate | pH 8.0, wild-type enzyme | Escherichia coli | |
| 5.3.1.28 | 1.2 | - |
D-sedoheptulose 7-phosphate | pH 8.0, mutant enzyme H61Q | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.3.1.28 | D-sedoheptulose 7-phosphate | Pseudomonas aeruginosa | first committed step in the formation of ADP-heptose | D-glycero-D-manno-heptose 7-phosphate | - |
? | |
| 5.3.1.28 | D-sedoheptulose 7-phosphate | Escherichia coli | first committed step in the formation of ADP-heptose | D-glycero-D-manno-heptose 7-phosphate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.3.1.28 | Escherichia coli | P63224 | - |
- |
| 5.3.1.28 | Pseudomonas aeruginosa | Q9HVZ0 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.3.1.28 | - |
Pseudomonas aeruginosa |
| 5.3.1.28 | - |
Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.3.1.28 | D-sedoheptulose 7-phosphate | first committed step in the formation of ADP-heptose | Pseudomonas aeruginosa | D-glycero-D-manno-heptose 7-phosphate | - |
? | |
| 5.3.1.28 | D-sedoheptulose 7-phosphate | first committed step in the formation of ADP-heptose | Escherichia coli | D-glycero-D-manno-heptose 7-phosphate | - |
? | |
| 5.3.1.28 | 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 | - |
? | |
| 5.3.1.28 | 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
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.3.1.28 | sedoheptulose-7-phosphate isomerase | - |
Pseudomonas aeruginosa |
| 5.3.1.28 | sedoheptulose-7-phosphate isomerase | - |
Escherichia coli |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.3.1.28 | 0.23 | - |
D-sedoheptulose 7-phosphate | pH 8.0, mutant enzyme H61Q | Escherichia coli | |
| 5.3.1.28 | 0.44 | - |
D-sedoheptulose 7-phosphate | pH 8.0, wild-type enzyme | Escherichia coli | |
| 5.3.1.28 | 0.45 | - |
D-sedoheptulose 7-phosphate | pH 8.0, mutant enzyme R69Q | Escherichia coli | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.3.1.28 | 8 | - |
assay at | Escherichia coli |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.3.1.28 | 0.2 | - |
D-sedoheptulose 7-phosphate | pH 8.0, mutant enzyme H61Q | Escherichia coli | |
| 5.3.1.28 | 0.5 | - |
D-sedoheptulose 7-phosphate | pH 8.0, wild-type enzyme | Escherichia coli | |
| 5.3.1.28 | 0.9 | - |
D-sedoheptulose 7-phosphate | pH 8.0, mutant enzyme R69Q | Escherichia coli | |
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