Glycine, serine and threonine metabolism
Penicillin and cephalosporin biosynthesis
pH dependence of catalysis of the monomer of hog kidney D-amino acid oxidase.
Chemical modification of D-amino acid oxidase. Amino acid sequence of the tryptic peptides containing tyrosine and lysine residues modified by fluorodinitrobenzene.
Identification of the histidine residue in D-amino acid oxidase that is covalently modified during inactivation by 5-dimethylaminonaphthalene-1-sulfonyl chloride.
MUTAGENESIS OF Y-55/M-110/H-217 TO SHOW THEY ARE NOT IN ACTIVE SITE
Effect of site-specific mutagenesis of tyrosine-55, methionine-110 and histidine-217 in porcine kidney D-amino acid oxidase on its catalytic function.
Two spectrophotometric assays for D-amino acid oxidase: for the study of distribution patterns.
Site-specific mutagenesis of lysine-204, tyrosine-224, tyrosine-228, and histidine-307 of porcine kidney D-amino acid oxidase and the implications as to its catalytic function.
Studies on Phe-228 and Leu-307 recombinant mutants of porcine kidney D-amino acid oxidase: expression, purification, and characterization.
Regional differences for the D-amino acid oxidase-catalysed oxidation of D-methionine in chicken small intestine.
Intrinsic primary, secondary, and solvent kinetic isotope effects on the reductive half-reaction of D-amino acid oxidase: evidence against a concerted mechanism.
Studies on the kinetic mechanism of pig kidney D-amino acid oxidase by site-directed mutagenesis of tyrosine 224 and tyrosine 228.
Structures of charge-transfer complexes of flavoenzyme D-amino acid oxidase: a study by resonance Raman spectroscopy and extended Huckel molecular orbital method.
Synthesis, characterization and preliminary crystallographic data of N6-(6-carbamoylhexyl)-FAD-D-amino-acid oxidase from pig kidney, a semi-synthetic oxidase.
Three-dimensional structure of porcine kidney D-amino acid oxidase at 3.0 A resolution.
Crystallization of expressed porcine kidney D-amino acid oxidase and preliminary X-ray crystallographic characterization.
Crystal structure of D-amino acid oxidase: a case of active site mirror-image convergent evolution with flavocytochrome b2.
Active site plasticity in D-amino acid oxidase: a crystallographic analysis.
Limited proteolysis and X-ray crystallography reveal the origin of substrate specificity and of the rate-limiting product release during oxidation of D-amino acids catalyzed by mammalian D-amino acid oxidase.
Structure of D-amino acid oxidase: new insights from an old enzyme.
Structural and mechanistic studies on D-amino acid oxidase x substrate complex: implications of the crystal structure of enzyme x substrate analog complex.
Glycerol-assisted restorative adjustment of flavoenzyme conformation perturbed by site-directed mutagenesis.
The role of a conserved histidine residue, His324, in Trigonopsis variabilis D-amino acid oxidase.
Three-dimensional structure of the purple intermediate of porcine kidney D-amino acid oxidase. Optimization of the oxidative half-reaction through alignment of the product with reduced flavin.
Substrate recognition and activation mechanism of D-amino acid oxidase: a study using substrate analogs.
Design and properties of human D-amino acid oxidase with covalently attached flavin.
The x-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation.
On the ligands in charge-transfer complexes of porcine kidney flavoenzyme D-amino acid oxidase in three redox states: a resonance Raman study.
First-principles molecular dynamics investigation of the D-amino acid oxidative half-reaction catalyzed by the flavoenzyme D-amino acid oxidase.
Yeast D-amino acid oxidase: structural basis of its catalytic properties.
On the mechanism of Rhodotorula gracilis D-amino acid oxidase: role of the active site serine 335.
Although the first domain of this enzyme is classified in CATH 3.40.50.720, it should be homologous to sarcosine oxidase (E.C. 1.5.3.1; D00041 in EzCatDB), and is re-classified into CATH 3.50.50.60 in this database. Although this enzyme is homologous to yeast counterpart (D00494 in EzCatDB), a set of catalytic residues is slightly different from the counterpart. The sidechain of Tyr224 plays a catalytic role as the counterpart of corresponding Ser335 in the yeast enzyme (see D00494) (see [15] & [26]). According to the literature [22], this enzyme catalyzes the following reactions: (A) Hydride transfer from D-amino acid to FAD, giving imino acid and FADH2 (reductive half-reaction). (B) Hydride transfer from FADH2 to O2, giving FAD and H2O2 (oxidative half-reaction). (C) Exchange of double-bonded atoms of the imino acid (Schiff-base deformation by water)