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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.168
-
 Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.1.168 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

EC Number Protein Variants Comment Organism
4.2.1.168 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

EC Number Organism UniProt Comment Textmining
4.2.1.168 Escherichia coli Q9F118
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.168 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

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

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.1.168 pyridoxamine 5'-phosphate
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
4.2.1.168 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