1.1.1.271	C109A	lower Km than wild-type enzyme	389518	
1.1.1.271	C109S	active site mutant, produces GDP-6-deoxy-D-altrose as its major product (75%) besides GDP-L-fucose (25%) out of GDP-4-keto-6-deoxy-D-mannose	698467	
1.1.1.271	C109S	produces GDP-6-deoxy-D-altrose as its major product, thus C-3'' epimerization occurs first and premature reduction of the GDP-4-keto-6-deoxy-D-altrose intermediate becomes competitive with GDP-L-fucose production. Results in the appearance of a kinetic isotope effect when [3''-2H]-GDP-6-deoxy-4-ketomannose is used as a substrate. The mutant catalyzes a rapid wash-in of solvent derived deuterium into the C-5'' position of GDP-fucose in the presence of NADP+	698467	
1.1.1.271	H179N	lower Km than wild-type enzyme	389518	
1.1.1.271	H179Q	is inactive, readily catalyzes the wash-out of deuterium from the C-3'' position of [3''-2H]-GDP-6-deoxy-4-keto-mannose	698467	
1.1.1.271	H179Q	the mutant catalyzes isotope exchange into starting material indicates that its active site has not been dramatically perturbed and it is still able to bind substrate and catalyze deprotonation events	698467	
1.1.1.271	K140R	higher Km than wild-type enzyme	389518	
1.1.1.271	K140S	higher Km than wild-type enzyme	389518	
1.1.1.271	additional information	effective GDP-L-fucose production in recombinant Escherichia coli by expression of GDP-D-mannose-4,6-dehydratase and GDP-4-keto-6-deoxymannose 3,5-epimerase 4-reductase, method optimization at 25°C and 0.1 mM isopropyl-beta-D-thioglucopyranoside, overview	677753	
1.1.1.271	R187A	lower Km than wild-type enzyme	389518	
1.1.1.271	S107A	lower Km than wild-type enzyme	389518	
1.1.1.271	Y136E	no enzymatic activity	389518