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Literature summary for 4.2.1.168 extracted from

  • Cook, P.; Holden, H.
    A structural study of GDP-4-keto-6-deoxy-D-mannose-3-dehydratase: Caught in the act of geminal diamine formation (2007), Biochemistry, 46, 14215-14224.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.1.168

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant H188K in the presence of alpha-ketoglutarate and pyridoxal 5'-phosphate, to 1.9 A resolution. The observed electron density is consistent with the formation of a geminal diamine intermediate formed by the reaction of an internal aldimine with glutamate Escherichia coli

Protein Variants

Protein Variants Comment Organism
H188K the active site histidine has been replaced with a lysine. The electron density reveals that the geminal diamine, a tetrahedral intermediate in the formation of pyridoxamine 5'-phosphate from pyridoxal 5'-phosphate, has been trapped within the active site region Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli Q9F118
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GDP-4-dehydro-alpha-D-rhamnose + L-glutamate
-
 Escherichia coli GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + 2-oxoglutarate + ammonia overall reaction ?

Synonyms

Synonyms Comment Organism
colD
-
 Escherichia coli
GDP-4-keto-6-deoxy-D-mannose-3-dehydratase
-
 Escherichia coli
WbdK
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxamine 5'-phosphate
-
 Escherichia coli

General Information

General Information Comment Organism
physiological function enzyme catalyzes the third step in the pathway to colitose, namely the PLP-dependent removal of the C3'-hydroxyl group from GDP-4-keto-6-deoxymannose Escherichia coli