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Literature summary extracted from

  • Wise, E.L.; Yew, W.S.; Gerlt, J.A.; Rayment, I.
    Structural evidence for a 1,2-enediolate intermediate in the reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase, a member of the orotidine 5'-monophosphate decarboxylase suprafamily (2003), Biochemistry, 42, 12133-12142.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.85 purified recombinant enzyme complexed with L-gulonate 6-phosphate, L-threonohydroxamate 4-phosphate, and L-xylitol 5-phosphate, analogues of the substrate, enediolate intermediate, and product, as well as with the product L-xylulose 5-phosphate, 15 mg/ml protein in 50 mM HEPES, pH 7.5, 5 mM MgCl2, 100 mM NaCl, micro-batch method, 0.01 ml protein solution mixed with equal volume of crystallization solution containing 16% monomethyl PEG 5000, 100 mM Bis-Tris propane, pH 7.0, and 5 mM MgCl2, with 25 mM ligand, X-ray diffraction structure determination and analysis at 1.2, 1.8, 1.7, and 1.8 A resolution, respectively Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.85 L-xylitol 5-phosphate binding structure Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.85 Mg2+ dependent on Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.85 3-dehydro-L-gulonate 6-phosphate + H+ Escherichia coli
-
L-xylulose 5-phosphate + CO2
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.85 Escherichia coli P39304
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.1.85 3-dehydro-L-gulonate 6-phosphate + H+ = L-xylulose 5-phosphate + CO2 active site structure, substrate binding structure, formation of a cis-1,2-enediolate anion intermediate, intermediate structure and reaction mechanism involving residues Lys64, Asp67, and His136, overview Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.85 3-dehydro-L-gulonate 6-phosphate + H+
-
Escherichia coli L-xylulose 5-phosphate + CO2
-
?
4.1.1.85 3-dehydro-L-gulonate 6-phosphate + H+ substrate binding structure Escherichia coli L-xylulose 5-phosphate + CO2
-
?

Synonyms

EC Number Synonyms Comment Organism
4.1.1.85 3-keto-L-gulonate 6-phosphate decarboxylase
-
Escherichia coli
4.1.1.85 KGPDC
-
Escherichia coli
4.1.1.85 More the enzyme belongs to the orotidine 5'-monophosphate decarboxylase OMPDC suprafamily, overview Escherichia coli