Literature summary for 4.1.1.85 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.

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	dependent on	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	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
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	a

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	-	?
3-dehydro-L-gulonate 6-phosphate + H+	substrate binding structure	Escherichia coli	L-xylulose 5-phosphate + CO2	-	?

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