about
Intermediates in the transformation of phosphonates to phosphate by bacteriaThe Enzyme Function Initiative.Structure-based activity prediction for an enzyme of unknown functionThe structure of carbamoyl phosphate synthetase determined to 2.1 A resolutionInactivation of the amidotransferase activity of carbamoyl phosphate synthetase by the antibiotic acivicinCarbamoyl-phosphate synthetase. Creation of an escape route for ammoniaStructural and kinetic studies of sugar binding to galactose mutarotase from Lactococcus lactisThe catalytic mechanism of galactose mutarotaseHigh-resolution X-ray structure of isoaspartyl dipeptidase from Escherichia coliStructural diversity within the mononuclear and binuclear active sites of N-acetyl-D-glucosamine-6-phosphate deacetylaseA Common Catalytic Mechanism for Proteins of the HutI Family †Structure of Diethyl Phosphate Bound to the Binuclear Metal Center of Phosphotriesterase † ‡Functional Annotation and Three-Dimensional Structure of Dr0930 from Deinococcus radiodurans , a Close Relative of Phosphotriesterase in the Amidohydrolase Superfamily † ‡Functional Identification of Incorrectly Annotated Prolidases from the Amidohydrolase Superfamily of Enzymes † ‡Functional Annotation of Two New Carboxypeptidases from the Amidohydrolase Superfamily of EnzymesAnnotating Enzymes of Uncertain Function: The Deacylation of d -Amino Acids by Members of the Amidohydrolase Superfamily ,The Mechanism of the Reaction Catalyzed by Uronate Isomerase Illustrates How an Isomerase May Have Evolved from a Hydrolase within the Amidohydrolase SuperfamilyStructure, Mechanism, and Substrate Profile for Sco3058: The Closest Bacterial Homologue to Human Renal Dipeptidase,The Hunt for 8-Oxoguanine DeaminaseDiscovery and Structure Determination of the Orphan Enzyme Isoxanthopterin Deaminase,Functional Identification and Structure Determination of Two Novel Prolidases from cog1228 in the Amidohydrolase Superfamily,Three-Dimensional Structure and Catalytic Mechanism of Cytosine DeaminaseRescue of the Orphan Enzyme Isoguanine DeaminaseEnzymes for the Homeland Defense: Optimizing Phosphotriesterase for the Hydrolysis of Organophosphate Nerve AgentsThe catalase activity of diiron adenine deaminaseStructural and Mechanistic Characterization of l -Histidinol Phosphate Phosphatase from the Polymerase and Histidinol Phosphatase Family of ProteinsStructure and Catalytic Mechanism of LigI: Insight into the Amidohydrolase Enzymes of cog3618 and Lignin DegradationMolecular Engineering of Organophosphate Hydrolysis Activity from a Weak Promiscuous Lactonase TemplateDeamination of 6-Aminodeoxyfutalosine in Menaquinone Biosynthesis by Distantly Related EnzymesProspecting for Unannotated Enzymes: Discovery of a 3′,5′-Nucleotide Bisphosphate Phosphatase within the Amidohydrolase SuperfamilySubstrate Deconstruction and the Nonadditivity of Enzyme RecognitionVariants of Phosphotriesterase for the Enhanced Detoxification of the Chemical Warfare Agent VRStructure of a Novel Phosphotriesterase from Sphingobium sp. TCM1: A Familiar Binuclear Metal Center Embedded in a Seven-Bladed β-Propeller Protein FoldStructural defects within the carbamate tunnel of carbamoyl phosphate synthetaseTunneling of intermediates in enzyme-catalyzed reactionsStructure-guided discovery of new deaminase enzymesStructural characterization and function determination of a nonspecific carboxylate esterase from the amidohydrolase superfamily with a promiscuous ability to hydrolyze methylphosphonate estersAnnotating enzymes of unknown function: N-formimino-L-glutamate deiminase is a member of the amidohydrolase superfamilyPa0148 from Pseudomonas aeruginosa catalyzes the deamination of adenineFunctional annotation and structural characterization of a novel lactonase hydrolyzing D-xylono-1,4-lactone-5-phosphate and L-arabino-1,4-lactone-5-phosphate.
P50
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P50
description
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Frank M Raushel
@ast
Frank M Raushel
@en
Frank M Raushel
@es
Frank M Raushel
@nl
type
label
Frank M Raushel
@ast
Frank M Raushel
@en
Frank M Raushel
@es
Frank M Raushel
@nl
prefLabel
Frank M Raushel
@ast
Frank M Raushel
@en
Frank M Raushel
@es
Frank M Raushel
@nl
P106
P21
P31
P496
0000-0002-5918-3089