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UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + NADPH + H+
UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NADP+ + H+
UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NAD(P)+
UDP-2-acetamido-2,6-beta-L-arabino-hexul-4-ose + NAD(P)H + H+
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + NADPH + H+
UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NADP+ + H+
-
Substrates: -
Products: enzyme WbjC is responsible for the reduction at C4 of UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose
?
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + NADPH + H+
UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NADP+ + H+
-
Substrates: -
Products: product of enzyme WbjC. WbjC is bifunctional, catalyzing C3 epimerization of UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose, the second intermediate of the pathway followed by reduction at C4
?
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + NADPH + H+
UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NADP+ + H+
-
Substrates: -
Products: product of enzyme WbjC. WbjC is bifunctional, catalyzing C3 epimerization of UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose, the second intermediate of the pathway followed by reduction at C4
?
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + NADPH + H+
UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NADP+ + H+
-
Substrates: -
Products: enzyme WbjC is responsible for the reduction at C4 of UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose
?
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + NADPH + H+
UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NADP+ + H+
Substrates: -
Products: enzyme Cap5F is responsible for the reduction at C4 of UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose
?
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + NADPH + H+
UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NADP+ + H+
Substrates: -
Products: reaction proceeeds via the intermediate UDP-2-acetamido-2,6-dideoxy-beta-L-lyxo-4-hexulose
?
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + NADPH + H+
UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NADP+ + H+
Substrates: -
Products: reaction proceeeds via the intermediate UDP-2-acetamido-2,6-dideoxy-beta-L-lyxo-4-hexulose
?
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + NADPH + H+
UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NADP+ + H+
Substrates: -
Products: enzyme Cap5F is responsible for the reduction at C4 of UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose
?
UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NAD(P)+
UDP-2-acetamido-2,6-beta-L-arabino-hexul-4-ose + NAD(P)H + H+
Substrates: part of the biosynthesis of UDP-N-acetyl-L-fucosamine
Products: -
?
UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NAD(P)+
UDP-2-acetamido-2,6-beta-L-arabino-hexul-4-ose + NAD(P)H + H+
Substrates: UDP-2-acetamido-2,6-dideoxy-beta-L-talose i.e. UDP-N-acetyl-beta-L-pneumosamine
Products: -
?
UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NAD(P)+
UDP-2-acetamido-2,6-beta-L-arabino-hexul-4-ose + NAD(P)H + H+
Substrates: part of the biosynthesis of UDP-N-acetyl-L-fucosamine
Products: -
?
UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NAD(P)+
UDP-2-acetamido-2,6-beta-L-arabino-hexul-4-ose + NAD(P)H + H+
Substrates: UDP-2-acetamido-2,6-dideoxy-beta-L-talose i.e. UDP-N-acetyl-beta-L-pneumosamine
Products: -
?
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UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NAD(P)+
UDP-2-acetamido-2,6-beta-L-arabino-hexul-4-ose + NAD(P)H + H+
UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NAD(P)+
UDP-2-acetamido-2,6-beta-L-arabino-hexul-4-ose + NAD(P)H + H+
Substrates: part of the biosynthesis of UDP-N-acetyl-L-fucosamine
Products: -
?
UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NAD(P)+
UDP-2-acetamido-2,6-beta-L-arabino-hexul-4-ose + NAD(P)H + H+
Substrates: part of the biosynthesis of UDP-N-acetyl-L-fucosamine
Products: -
?
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physiological function
involved in biosynthesis of N-acetyl-L-fucosamine. Enzyme Cap5E catalyzes 4,6-dehydration of UDP-N-acetyl-Dglucosamine and 3- and 5-epimerization to yield a mixture of three keto-deoxy-sugars. UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose is subsequently reduced at C4 to UDP-2-acetamido-2,6-dideoxy-L-talose by Cap5F. Incubation of UDP-2-acetamido-2,6-dideoxy-L-talose with Cap5G results in 2-epimerization to N-acetyl-L-fucosamine
physiological function
-
involved in biosynthesis of N-acetyl-L-fucosamine. Enzyme WbjB catalyzes 4,6-dehydration of UDP-N-acetyl-Dglucosamine and 3- and 5-epimerization to yield a mixture of three keto-deoxy-sugars. UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose is subsequently reduced at C4 to UDP-2-acetamido-2,6-dideoxy-L-talose by WbjC. Incubation of UDP-2-acetamido-2,6-dideoxy-L-talose with WbjD results in 2-epimerization to N-acetyl-L-fucosamine
physiological function
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involved in biosynthesis of N-acetyl-L-fucosamine. Enzyme Cap5E catalyzes 4,6-dehydration of UDP-N-acetyl-Dglucosamine and 3- and 5-epimerization to yield a mixture of three keto-deoxy-sugars. UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose is subsequently reduced at C4 to UDP-2-acetamido-2,6-dideoxy-L-talose by Cap5F. Incubation of UDP-2-acetamido-2,6-dideoxy-L-talose with Cap5G results in 2-epimerization to N-acetyl-L-fucosamine
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physiological function
-
involved in biosynthesis of N-acetyl-L-fucosamine. Enzyme WbjB catalyzes 4,6-dehydration of UDP-N-acetyl-Dglucosamine and 3- and 5-epimerization to yield a mixture of three keto-deoxy-sugars. UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose is subsequently reduced at C4 to UDP-2-acetamido-2,6-dideoxy-L-talose by WbjC. Incubation of UDP-2-acetamido-2,6-dideoxy-L-talose with WbjD results in 2-epimerization to N-acetyl-L-fucosamine
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F297Y
mutation in the second co-ordination sphere of Zn2+, mutant exerts a minor effect on catalytic activity
H290L
mutation in he coordination sphere of Zn2+. Mutant maintains a native-like dimeric conformation in solution, but does not generate a final product
H337L
mutant displays diminished thermal stability
S94A/Y103A
catalytic site of the short-chain dehydrogenase/reductase domain. Mutant maintains a native-like dimeric conformation in solution, but does not generate a final product. Addition of the reductase domain rescue the enzymatic activity
T364Y F297Y
mutation in the second co-ordination sphere of Zn2+, mutant exerts a minor effect on catalytic activity
F297Y
-
mutation in the second co-ordination sphere of Zn2+, mutant exerts a minor effect on catalytic activity
-
H290L
-
mutation in he coordination sphere of Zn2+. Mutant maintains a native-like dimeric conformation in solution, but does not generate a final product
-
H337L
-
mutant displays diminished thermal stability
-
S94A/Y103A
-
catalytic site of the short-chain dehydrogenase/reductase domain. Mutant maintains a native-like dimeric conformation in solution, but does not generate a final product. Addition of the reductase domain rescue the enzymatic activity
-
T364Y F297Y
-
mutation in the second co-ordination sphere of Zn2+, mutant exerts a minor effect on catalytic activity
-
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Miyafusa, T.; Tanaka, Y.; Kuroda, M.; Ohta, T.; Tsumoto, K.
Expression, purification, crystallization and preliminary diffraction analysis of CapF, a capsular polysaccharide-synthesis enzyme from Staphylococcus aureus
Acta Crystallogr. Sect. F
64
512-515
2008
Staphylococcus aureus (A0A0H3JP37), Staphylococcus aureus ATCC 700699 (A0A0H3JP37)
brenda
Mulrooney, E.F.; Poon, K.K.; McNally, D.J.; Brisson, J.R.; Lam, J.S.
Biosynthesis of UDP-N-acetyl-L-fucosamine, a precursor to the biosynthesis of lipopolysaccharide in Pseudomonas aeruginosa serotype O11
J. Biol. Chem.
280
19535-19542
2005
Pseudomonas aeruginosa, Pseudomonas aeruginosa O11
brenda
Miyafusa, T.; Caaveiro, J.M.; Tanaka, Y.; Tsumoto, K.
Crystal structure of the enzyme CapF of Staphylococcus aureus reveals a unique architecture composed of two functional domains
Biochem. J.
443
671-680
2012
Staphylococcus aureus (A0A0H3JP37), Staphylococcus aureus ATCC 700699 (A0A0H3JP37)
brenda
Kneidinger, B.; ORiordan, K.; Li, J.; Brisson, J.; Lee, J.; Lam, J.
Three highly conserved proteins catalyze the conversion of UDP-N-acetyl-D-glucosamine to precursors for the biosynthesis of O antigen in Pseudomonas aeruginosa O11 and capsule in Staphylococcus aureus type 5: Implications for the UDP-N-acetyl-L-fucosamine
J. Biol. Chem.
278
3615-3627
2003
Pseudomonas aeruginosa, Pseudomonas aeruginosa O11, Staphylococcus aureus (P95700), Staphylococcus aureus, Staphylococcus aureus Newman (P95700)
brenda