Information on EC 1.1.1.367 - UDP-2-acetamido-2,6-beta-L-arabino-hexul-4-ose reductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.367
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RECOMMENDED NAME
GeneOntology No.
UDP-2-acetamido-2,6-beta-L-arabino-hexul-4-ose reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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+
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
UDP-2-acetamido-2,6-dideoxy-L-talose:NADP+ oxidoreductase
Part of the biosynthesis of UDP-N-acetyl-L-fucosamine. Isolated from the bacteria Pseudomonas aeruginosa and Staphylococcus aureus.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + NADPH + H+
UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NADP+ + H+
show the reaction diagram
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+
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
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cofactor is essential only for the reduction reaction, NAPH binding is enthalpy-driven
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
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the C-terminal domain of the enzyme displays a standard cupin fold with a Zn2+ ion bound deep in the binding pocket of the beta-barrel
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method, optimization of the crystallization conditions by differential scanning calorimetry affords a crystal of selenomethionine-substituted enzyme that diffracts to a resolution of 2.80 A. The crystals belong to space group P3(2)21, with unit-cell parameters a = b = 119.6, c = 129.5 A
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in an open form of the apoenzyme. Enzyme CapF is a homodimer displaying a characteristic dumb-bell-shaped architecture composed of two domains. The N-terminal domain (residues 1-252) adopts a Rossmann fold belonging to the short-chain dehydrogenase/reductase family of proteins. The C-terminal domain (residues 252-369) displays a standard cupin fold with a Zn2+ ion bound deep in the binding pocket of the beta-barrel. The cupin domain is necessary for the C3-epimerization of UDP-4-hexulose. The N-terminal domain catalyses the NADPH-dependent reduction of the intermediate species generated by the cupin domain. A thermodynamic switch governs the attachment and release of the coenzyme NADPH during each catalytic cycle. suggesting that the binding of coenzyme to CapF facilitates a disorder-to-order transition in the catalytic loop of the reductase (N-terminal) domain
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 40% glycerol, stable for several weeks
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F297Y
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mutation in the second co-ordination sphere of Zn2+, mutant exerts a minor effect on catalytic activity
H290L
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mutation in he coordination sphere of Zn2+. Mutant maintains a native-like dimeric conformation in solution, but does not generate a final product
H337L
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mutant displays diminished thermal stability
S94A/Y103A
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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
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mutation in the second co-ordination sphere of Zn2+, mutant exerts a minor effect on catalytic activity
F297Y
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mutation in the second co-ordination sphere of Zn2+, mutant exerts a minor effect on catalytic activity
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H290L
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mutation in he coordination sphere of Zn2+. Mutant maintains a native-like dimeric conformation in solution, but does not generate a final product
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H337L
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mutant displays diminished thermal stability
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S94A/Y103A
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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
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T364Y F297Y
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mutation in the second co-ordination sphere of Zn2+, mutant exerts a minor effect on catalytic activity
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