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Literature summary for 1.1.1.169 extracted from

  • Ciulli, A.; Lobley, C.M.; Tuck, K.L.; Smith, A.G.; Blundell, T.L.; Abell, C.
    pH-tuneable binding of 2-phospho-ADP-ribose to ketopantoate reductase: a structural and calorimetric study (2007), Acta Crystallogr. Sect. D, 63, 171-178.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.169

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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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Organism

Organism UniProt Comment Textmining
Escherichia coli P0A9J4 gene panE
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-dehydropantoate + NADPH
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 Escherichia coli (R)-pantoate + NADP+
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 ?
2-dehydropantoate + NADPH the enzyme is involved in the biosynthesis of pantothenate, i.e. vitamin B5 Escherichia coli (R)-pantoate + NADP+
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 ?
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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Synonyms

Synonyms Comment Organism
ketopantoate reductase
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 Escherichia coli
KPR
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 Escherichia coli
More KPR belongs to the 6-phosphogluconate dehydrogenase superfamily in the SCOP database Escherichia coli

Cofactor

Cofactor Comment Organism Structure
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