• Publications
  • Influence
The Path from β-Carotene to Carlactone, a Strigolactone-Like Plant Hormone
Knowledge of the structure of carlactone will be crucial for understanding the biology of strigolactones and may have applications in combating parasitic weeds.
The structure of L‐amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site
A mirror‐symmetrical relationship between the two substrate‐binding sites is observed which facilitates enantiomeric selectivity while preserving a common arrangement of the atoms involved in catalysis.
Mechanisms of flavoprotein-catalyzed reactions.
This review describes the best studied of Flavoproteins mechanisms and discusses factors possibly governing reactivity and specificity.
Acyl-CoA dehydrogenases. A mechanistic overview.
This work discusses the main factors that bring about catalysis, promote specificity and determine the selective transfer of electrons to electron transferring flavoprotein in medium chain acyl-CoA dehydrogenase.
Purification and properties of prostaglandin 9-ketoreductase from pig and human kidney. Identity with human carbonyl reductase.
From comparison of several properties (catalytical, structural and immunological properties), it is concluded that PG-9-KR and carbonyl reductase are identical enzymes.
Structure and characterization of the glycan moiety of L-amino-acid oxidase from the Malayan pit viper Calloselasma rhodostoma.
The glycosylation of L-amino-acid oxidase from the venom of the Malayan pit viper is remarkably homogeneous with the major oligosaccharide accounting for approximately 90% of the total sugar content.
The x-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation.
The very high-resolution structures of yeast DAAO complexed with d-alanine, d-trifluoroalanines, and l-lactate provide strong evidence for hydride transfer as the mechanism of dehydrogenation, and point to orbital orientation/steering as the major factor in catalysis.
Yeast D-amino acid oxidase: structural basis of its catalytic properties.
Oxygen Access to the Active Site of Cholesterol Oxidase through a Narrow Channel Is Gated by an Arg-Glu Pair*
The structure suggests that Glu475, located at the active site cavity, may act as the base for both the oxidation and the isomerization steps of the catalytic reaction, which provides an explanation for the biphasic mode of reaction with dioxygen and the ping-pong kinetic mechanism exhibited by the enzyme.
Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity.
Solvent accessible space at the "midsection" of the active site cavity, where the C alpha-C beta bond of the thioester substrate and the isoalloxazine ring of the FAD are located, is larger in the double mutant than in the wild type enzyme, implying greater O2 accessibility in the mutant which might account for the higher oxygen reactivity.