Literature summary for 4.1.1.85 extracted from

Wise, E.L.; Yew, W.S.; Gerlt, J.A.; Rayment, I.
Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: crystallographic evidence for a proton relay system in the active site of 3-keto-L-gulonate 6-phosphate decarboxylase (2004), Biochemistry, 43, 6438-6446.

Cloned(Commentary)

Cloned (Comment)	Organism
expression of mutant enzymes in strain BLR(DE3)recA-strain	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant mutant enzymes K64A, H136A, E112Q, and E112Q/H136A, in complex with reaction intermediate analogue L-threonohydroxamate 4-phosphate, 15 mg/ml protein in 50 mM HEPES, pH 7.5, 5 mM MgCl2, 100 mM NaCl, 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, 5 mM MgCl2, and 25 mM L-threonohydroxamate 4-phosphate, X-ray diffraction structure determination and analysis at 1.7, 1.9, 1.8, and 1.9 A resolution, respectively	Escherichia coli

Crystallization (Comment)

Organism

purified recombinant mutant enzymes K64A, H136A, E112Q, and E112Q/H136A, in complex with reaction intermediate analogue L-threonohydroxamate 4-phosphate, 15 mg/ml protein in 50 mM HEPES, pH 7.5, 5 mM MgCl2, 100 mM NaCl, 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, 5 mM MgCl2, and 25 mM L-threonohydroxamate 4-phosphate, X-ray diffraction structure determination and analysis at 1.7, 1.9, 1.8, and 1.9 A resolution, respectively

Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
E112Q	site-directed mutagenesis, crystal structure determination and analysis, the mutant enzyme shows altered reaction intermediate binding at the active site, reaction mechanism, and stereochemistry	Escherichia coli
E112Q/H136A	site-directed mutagenesis, crystal structure determination and analysis, the mutant enzyme shows altered reaction intermediate binding at the active site, reaction mechanism, and stereochemistry	Escherichia coli
H136A	site-directed mutagenesis, crystal structure determination and analysis, the mutant enzyme shows altered reaction intermediate binding at the active site, reaction mechanism, and stereochemistry	Escherichia coli
K64A	site-directed mutagenesis, crystal structure determination and analysis, the mutant enzyme shows altered reaction intermediate binding at the active site, reaction mechanism, and stereochemistry	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	formation and stabilization of an 1,2-enediolate anion intermediate, protonation of the intermediate involving residues Glu112, His136, and Arg139, active site structure-function relationship, 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	-	?

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	Escherichia coli