Literature summary for 4.2.1.168 extracted from

Alam, J.; Beyer, N.; Liu, H.W.
Biosynthesis of colitose: expression, purification, and mechanistic characterization of GDP-4-keto-6-deoxy-D-mannose-3-dehydrase (ColD) and GDP-L-colitose synthase (ColC) (2004), Biochemistry, 43, 16450-16460.

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Organism

Organism	UniProt	Comment	Textmining
Yersinia pseudotuberculosis	G4WJD4	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
GDP-4-dehydro-alpha-D-rhamnose + L-glutamate	-	Yersinia pseudotuberculosis	GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + 2-oxoglutarate + ammonia	-	?
additional information	enzyme functions as GDP-4-keto-6-deoxy-D-mannose-3-dehydrase responsible for C-3 deoxygenation of GDP-4-keto-6-deoxy-D-mannose. The enzyme is coenzyme B6-dependent and catalysis is initiated by a transamination step in which pyridoxal 5'-phosphate is converted to pyridoxamine 5'-phosphate in the presene of L-glutamate. This coenzyme forms a Schiff base with the keto sugar substrate and the resulting adduct undergoes a pyridoxamine 5'-phosphate-mediated beta-dehydration reaction to give a sugar enamine intermediate, which after tautomerization and hydrolysis to release ammonia yields GDP-4-keto-3,6-dideoxy-D-mannose as the product	Yersinia pseudotuberculosis	?	-	?

Synonyms

Synonyms	Comment	Organism
colD	-	Yersinia pseudotuberculosis

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Release 2023.1 (January 2023)