Literature summary for 4.2.1.168 extracted from

Cook, P.; Thoden, J.; Holden, H.
The structure of GDP-4-keto-6-deoxy-D-mannose-3-dehydratase: A unique coenzyme B6-dependent enzyme (2006), Protein Sci., 15, 2093-2106.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
the two subunits of the protein form a tight dimer. The PLP-binding pocket is formed primarily by one subunit, with a loop from Phe 240 to Glu 253 in the second subunit, that completes the active site architecture. The hydrated form of PLP is observed. Amino acid residues involved in anchoring the cofactor to the protein include Gly56, Ser57, Asp159, Glu162, and Ser183 from one subunit and Asn248 from the second monomer. His188 is the active site base required for catalysis	Escherichia coli

Crystallization (Comment)

Organism

the two subunits of the protein form a tight dimer. The PLP-binding pocket is formed primarily by one subunit, with a loop from Phe 240 to Glu 253 in the second subunit, that completes the active site architecture. The hydrated form of PLP is observed. Amino acid residues involved in anchoring the cofactor to the protein include Gly56, Ser57, Asp159, Glu162, and Ser183 from one subunit and Asn248 from the second monomer. His188 is the active site base required for catalysis

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	Q9F118	-	-

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Release 2023.1 (January 2023)