EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.1.1.169 | purified recombinant His6-tagged enzyme in complex with 2'-monophosphoadenosine 5'-diphosphoribose, 4°C, 10-15 mg/ml protein with NADPH and pantoate at a final ligand:protein ratio of 2:1 and 5:1, respectively, mixing with 10% 2-methyl-2,4-pentanediol buffered with 0.1 M sodium acetate pH 4.0-5.0, X-ray diffraction structure determination and analysis at 1.95-2.0 A resolution | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.169 | 2-dehydropantoate + NADPH | Escherichia coli | the enzyme is involved in the biosynthesis of pantothenate, i.e. vitamin B5 | (R)-pantoate + NADP+ | - |
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EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.169 | Escherichia coli | P0A9J4 | gene panE | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.169 | 2-dehydropantoate + NADPH | - |
Escherichia coli | (R)-pantoate + NADP+ | - |
? | |
1.1.1.169 | 2-dehydropantoate + NADPH | the enzyme is involved in the biosynthesis of pantothenate, i.e. vitamin B5 | Escherichia coli | (R)-pantoate + NADP+ | - |
? | |
1.1.1.169 | additional information | complex formation of 2'-monophosphoadenosine 5'-diphosphoribose upon incubation of NADPH at pH 5.0, structure analysis, overview | Escherichia coli | ? | - |
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EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.169 | ketopantoate reductase | - |
Escherichia coli |
1.1.1.169 | KPR | - |
Escherichia coli |
1.1.1.169 | More | KPR belongs to the 6-phosphogluconate dehydrogenase superfamily in the SCOP database | Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.169 | NADP+ | dependent on, binding structure of 2'-monophosphoadenosine 5'-diphosphoribose, a fragment of NADP+ that lacks the nicotinamide ring, bound at the enzyme active site in the opposite orientation to that observed for NADP+, with the adenine ring occupying the lipophilic nicotinamide pocket, binding structure, overview | Escherichia coli |