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Literature summary for 4.1.1.85 extracted from

  • Wise, E.L.; Yew, W.S.; Akana, J.; Gerlt, J.A.; Rayment, I.
    Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: structural basis for catalytic promiscuity in wild-type and designed mutants of 3-keto-L-gulonate 6-phosphate decarboxylase (2005), Biochemistry, 44, 1816-1823.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of N-terminally His10-tagged wild-type and mutant enzymes in enzyme-deficient strain BLR(DE3) Escherichia coli K-12

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant wild-type and mutant enzymes E112D/R139V, E112D/T169A, and E112D/R139V/T169A, 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, 5 mM MgCl2, and 25 mM L-xylulose 5-phosphate or D-ribulose 5-phosphate, cryoprotection of crystals in 15% monomethylPEG 5000, 100 mM PIPES, pH 7.0, 15% ethylene glycol, 200 mM NaCl, and 50 mM L-threonohydroxamate 4-phosphate or 50 mM D-ribulose 5-phosphate, X-ray diffraction structure determination and analysis at 1.6-1.8 A resolution, molecular replacement Escherichia coli K-12

Protein Variants

Protein Variants Comment Organism
E112D/R139V site-directed mutagenesis, mutations alter the Escherichia coli residues to those of Methylomonas aminofaciens D-arabino-hex-3-ulose 6-phosphate synthase, a homologous enzyme, also altering the enzyme activity of the 3-keto-L-gulonate 6-phosphate decarboxylase performing th Mg2+-dependent aldol condensation between formaldehyde and D-ribulose 5-phosphate with highly increased activity compared to the wild-type enzyme Escherichia coli K-12
E112D/R139V/T169A site-directed mutagenesis, mutations alter the Escherichia coli residues to those of Methylomonas aminofaciens D-arabino-hex-3-ulose 6-phosphate synthase, a homologous enzyme, also altering the enzyme activity of the 3-keto-L-gulonate 6-phosphate decarboxylase performing th Mg2+-dependent aldol condensation between formaldehyde and D-ribulose 5-phosphate with highly increased activity compared to the wild-type enzyme Escherichia coli K-12
E112D/T169A site-directed mutagenesis, mutations alter the Escherichia coli residues to those of Methylomonas aminofaciens D-arabino-hex-3-ulose 6-phosphate synthase, a homologous enzyme, also altering the enzyme activity of the 3-keto-L-gulonate 6-phosphate decarboxylase performing th Mg2+-dependent aldol condensation between formaldehyde and D-ribulose 5-phosphate with highly increased activity compared to the wild-type enzyme Escherichia coli K-12

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 K-12
-
L-xylulose 5-phosphate + CO2
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli K-12 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, structure-function relationship, overview Escherichia coli K-12

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-dehydro-L-gulonate 6-phosphate + H+
-
Escherichia coli K-12 L-xylulose 5-phosphate + CO2
-
?
additional information the enzyme also performs the Methylomonas aminofaciens D-arabino-hex-3-ulose 6-phosphate synthase reaction with low activity catalyzing Mg2+-dependent aldol condensation between formaldehyde and D-ribulose 5-phosphate, while the Methylomonas aminofaciens enzyme also performs the 3-keto-L-gulonate 6-phosphate decarboxylase reaction, overview Escherichia coli K-12 ?
-
?

Synonyms

Synonyms Comment Organism
3-keto-L-gulonate 6-phosphate decarboxylase
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Escherichia coli K-12
KGPDC
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Escherichia coli K-12
More the enzyme belongs to the orotidine 5'-monophosphate decarboxylase OMPDC suprafamily Escherichia coli K-12