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Literature summary for 1.1.1.367 extracted from

  • 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 (2012), Biochem. J., 443, 671-680.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Staphylococcus aureus

Protein Variants

Protein Variants Comment Organism
F297Y mutation in the second co-ordination sphere of Zn2+, mutant exerts a minor effect on catalytic activity Staphylococcus aureus
H290L mutation in he coordination sphere of Zn2+. Mutant maintains a native-like dimeric conformation in solution, but does not generate a final product Staphylococcus aureus
H337L mutant displays diminished thermal stability Staphylococcus aureus
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 Staphylococcus aureus
T364Y F297Y mutation in the second co-ordination sphere of Zn2+, mutant exerts a minor effect on catalytic activity Staphylococcus aureus

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ 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 Staphylococcus aureus

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus A0A0H3JP37
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Staphylococcus aureus ATCC 700699 A0A0H3JP37
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose + NADPH + H+
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Staphylococcus aureus UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NADP+ + H+ 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+
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Staphylococcus aureus ATCC 700699 UDP-2-acetamido-2,6-dideoxy-beta-L-talose + NADP+ + H+ reaction proceeeds via the intermediate UDP-2-acetamido-2,6-dideoxy-beta-L-lyxo-4-hexulose ?

Synonyms

Synonyms Comment Organism
Cap5F
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Staphylococcus aureus
CapF
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Staphylococcus aureus
capsular polysaccharide synthesis enzyme
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Staphylococcus aureus

Cofactor

Cofactor Comment Organism Structure
NADPH cofactor is essential only for the reduction reaction, NAPH binding is enthalpy-driven Staphylococcus aureus