4.1.1.85: 3-dehydro-L-gulonate-6-phosphate decarboxylase
This is an abbreviated version!
For detailed information about 3-dehydro-L-gulonate-6-phosphate decarboxylase, go to the full flat file.
Word Map on EC 4.1.1.85
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4.1.1.85
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ompdc
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orotidine
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5'-monophosphate
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suprafamily
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mg2+-dependent
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enediolate
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l-ascorbate
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gerlt
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wise
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beta-strands
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cis-enediolate
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rayment
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d-ribulose
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ump
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bidentate
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d-xylulose
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babbitt
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ion-independent
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vinyl
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3-epimerase
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conscripting
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methylomonas
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hydrogen-bonded
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lys
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4-phosphate
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manuscript
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relay
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bacteriol
- 4.1.1.85
- ompdc
- orotidine
-
5'-monophosphate
-
suprafamily
-
mg2+-dependent
-
enediolate
- l-ascorbate
-
gerlt
-
wise
-
beta-strands
-
cis-enediolate
-
rayment
- d-ribulose
- ump
-
bidentate
- d-xylulose
-
babbitt
-
ion-independent
-
vinyl
-
3-epimerase
-
conscripting
-
methylomonas
-
hydrogen-bonded
- lys
- 4-phosphate
-
manuscript
-
relay
-
bacteriol
Reaction
Synonyms
3-keto-L-gulonate 6-phosphate decarboxylase, KGPDC, More, SgaH, SgbH, UlaD
ECTree
4.1.1.85 3-dehydro-L-gulonate-6-phosphate decarboxylaseAdvanced search results
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results (Reaction
Reaction on EC 4.1.1.85 - 3-dehydro-L-gulonate-6-phosphate decarboxylase
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REACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
3-dehydro-L-gulonate 6-phosphate + H+ = L-xylulose 5-phosphate + CO2
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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
3-dehydro-L-gulonate 6-phosphate + H+ = L-xylulose 5-phosphate + CO2
active site structure, substrate binding structure, structure-function relationship, overview
3-dehydro-L-gulonate 6-phosphate + H+ = L-xylulose 5-phosphate + CO2
catalytic mechanism, formation and Mg2+-stabilization of an cis-1,2-enediolate anion intermediate, important residues for the stereospecific exchange of the pro-1S hydrogen are Lys64, Asp67, Glu112, Arg139, and Lys64, the latter stabilizes the intermediate via hydrogen bonds to O1 and O2 of the intermediate involving conserved active site residue Asp67, His136 takes part in hydrogen exchange with solvent of the 1-hydroxymethylene group of the product, overview
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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
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
