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The Path from β-Carotene to Carlactone, a Strigolactone-Like Plant Hormone
Making Carlactone Germination of parasitic witchweeds depends on strigolactones, which also regulate plant branching and signal in the context of mycorrhizal symbioses. The biosynthetic pathways thatExpand
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The structure of L‐amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site
The structure of L‐amino acid oxidase (LAAO) from Calloselasma rhodostoma has been determined to 2.0 Å resolution in the presence of two ligands: citrate and o‐aminobenzoate (AB). The protomerExpand
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Mechanisms of flavoprotein-catalyzed reactions.
Flavoproteins are a class of enzymes catalyzing a very broad spectrum of redox processes by different chemical mechanisms. This review describes the best studied of these mechanisms and discussesExpand
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Acyl-CoA dehydrogenases. A mechanistic overview.
Acyl-CoA dehydrogenases constitute a family of flavoproteins that catalyze the alpha,beta-dehydrogenation of fatty acid acyl-CoA conjugates. While they differ widely in their specificity, they shareExpand
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Purification and properties of prostaglandin 9-ketoreductase from pig and human kidney. Identity with human carbonyl reductase.
Prostaglandin 9-ketoreductase (PG-9-KR) was purified from pig kidney to homogeneity, as judged by SDS/PAGE using an improved procedure. The enzyme is pro-S stereoselective with regard to hydrogenExpand
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The x-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation.
Flavin is one of the most versatile redox cofactors in nature and is used by many enzymes to perform a multitude of chemical reactions. d-Amino acid oxidase (DAAO), a member of the flavoproteinExpand
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Structure and characterization of the glycan moiety of L-amino-acid oxidase from the Malayan pit viper Calloselasma rhodostoma.
Ophidian L-amino-acid oxidase (L-amino-acid oxygen:oxidoreductase, deaminating, EC is found in the venom of many poisonous snakes (crotalids, elapids and viperids). This FAD-dependentExpand
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Oxygen Access to the Active Site of Cholesterol Oxidase through a Narrow Channel Is Gated by an Arg-Glu Pair*
Cholesterol oxidase is a monomeric flavoenzyme that catalyzes the oxidation and isomerization of cholesterol to cholest-4-en-3-one. Two forms of the enzyme are known, one containing the cofactorExpand
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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.
Crystal structures of the wild type human medium-chain acyl-CoA dehydrogenase (MCADH) and a double mutant in which its active center base-arrangement has been altered to that of long chain acyl-CoAExpand
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A hydrophobic sequence motif common to N-hydroxylating enzymes.
The first committed step in the biosynthesis of various bacterial and fur,gal siderophores (low-molecular-weight iron chelators that are produc~ in response '~o iron deficiency) of the hydroxamateExpand
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