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Literature summary for 1.1.1.336 extracted from

  • Pampa, K.J.; Lokanath, N.K.; Girish, T.U.; Kunishima, N.; Rai, V.R.
    Crystal structure of product-bound complex of UDP-N-acetyl-D-mannosamine dehydrogenase from Pyrococcus horikoshii OT3 (2014), Biochem. Biophys. Res. Commun., 453, 662-667.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of the enzyme bound to the product UDP-N-acetyl-alpha-D-mannosaminuronate by X-ray diffraction to resolution of 1.55 A. Crystal structures reveal a tight dimeric polymer chains with product-bound in all the structures. The catalytic residues Cys258 and Lys204 are conserved. The Cys258 acts as catalytic nucleophile and Lys204 as acid/base catalyst. The product directly interacts with residues Arg211, Thr249, Arg244, Gly255, Arg289, Lys319 and Arg398. The SeMet-substituted enzyme is crystallized using microbatch sitting method under reservoir solution condition 10% (w/v) PEG 8000, 8% (v/v) ethylene glycol and 0.1 M HEPES, pH 7.5 Pyrococcus horikoshii

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii
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Pyrococcus horikoshii OT-3
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-
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Purification (Commentary)

Purification (Comment) Organism
-
Pyrococcus horikoshii

Subunits

Subunits Comment Organism
dimer monomers aggregate to dimeric form with major interactions from oligomerization domain residues Pyrococcus horikoshii

Synonyms

Synonyms Comment Organism
UDP-D-ManNAcDH
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Pyrococcus horikoshii