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Literature summary for 4.1.1.85 extracted from

  • Wise, E.; Yew, W.S.; Babbitt, P.C.; Gerlt, J.A.; Rayment, I.
    Homologous (beta/alpha)8-barrel enzymes that catalyze unrelated reactions: orotidine 5'-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase (2002), Biochemistry, 41, 3861-3869.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene ulaD, expression as His-tagged protein in strain BL21(DE3), and as selenomethionine-labeled enzyme Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant wild-type and selenomethionine-labeled enzymes, free or complexed with inhibitor L-gulonate 6-phosphate, 15 mg/ml protein in 50 mM HEPES, pH 7.5, 5 mM MgCl2, 100 mM NaCl, room temperature, micro-batch method, 0.01 ml protein solution mixed with equal volume of crystallization solution containing 18% monomethyl PEG 5000, 50 mM NaH2PO4, 50 mM K2HPO4, and 50 mM Bis-Tris propane, pH 7.0, with or without 20 mM inhibitor L-gulonate 6-phosphate, crystals appear a few days after microseeding, growing for 1 week, X-ray diffraction structure determination and analysis at 2.0 A resolution Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
L-gulonate 6-phosphate binding structure involving Glu33 and Asp62 and Mg2+ Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ dependent on, binding structure involving Glu33 and Asp62, overview Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-dehydro-L-gulonate 6-phosphate + H+ Escherichia coli
-
L-xylulose 5-phosphate + CO2
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P39304 gene ulaD
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged UlaD from strain BL21(DE3), the His-tag is removed by thrombin Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
3-dehydro-L-gulonate 6-phosphate + H+ = L-xylulose 5-phosphate + CO2 formation and stabilization of an enediolate anion intermediate is part of reaction mechanism, mechanism overview, the active site is located at the dimer interface, structure-function relationship, overview Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-dehydro-L-gulonate 6-phosphate + H+
-
Escherichia coli L-xylulose 5-phosphate + CO2
-
?

Subunits

Subunits Comment Organism
dimer (beta/alpha)8-barrel enzyme, the active site is located at the dimer interface Escherichia coli

Synonyms

Synonyms Comment Organism
3-keto-L-gulonate 6-phosphate decarboxylase
-
Escherichia coli
KGPDC
-
Escherichia coli
More the enzyme belongs to the orotidine 5'-monophosphate decarboxylase OMPDC suprafamily, overview Escherichia coli