Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Weidner, A.; Neumann, P.; Wille, G.; Stubbs, M.T.; Tittmann, K.
    Crystallization and preliminary X-ray diffraction analysis of full-length and proteolytically activated pyruvate oxidase from Escherichia coli (2008), Acta Crystallogr. Sect. F, 64, 179-181.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.3.3 overexpressed in Escherichia coli strain ZK126 carrying the plasmid pYYC102 which encodes the poxB gene Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.2.3.3 the full-length form and a proteolytically activated C-terminal truncation variant which lacks the last 23 amino acids, by the hanging-drop vapour-diffusion method using either protamine sulfate (fulllength POX) or 2-methyl-2,4-pentanediol (DELTA23 POX) as precipitants. To 2.9 A resolution. Fulllength POX crystallizes in the tetragonal space group P43212 with two monomers per asymmetric unit, the crystals of DELTA23 POX belong to the orthorhombic space group P212121 and contain 12 monomers per asymmetric unit Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Organism

EC Number Organism UniProt Comment Textmining
1.2.3.3 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.3.3 by anion-exchange chromatography, more than 95% pure Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.3.3 pyruvate + phosphate + ferricyanide + H2O
-
 Escherichia coli acetyl phosphate + ferrocyanide + H2O2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.2.3.3 POX
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.3.3 FAD
-
 Escherichia coli