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Two Structures of a Thiazolinyl Imine Reductase from Yersinia enterocolitica Provide Insight into Catalysis and Binding to the Nonribosomal Peptide Synthetase Module of HMWP1How pH Modulates the Reactivity and Selectivity of a Siderophore-Associated Flavin MonooxygenaseYou are lost without a map: Navigating the sea of protein structuresModification of residue 42 of the active site loop with a lysine-mimetic side chain rescues isochorismate-pyruvate lyase activity in Pseudomonas aeruginosa PchB.Structure of an Aspergillus fumigatus old yellow enzyme (EasA) involved in ergot alkaloid biosynthesis.Expanding the results of a high throughput screen against an isochorismate-pyruvate lyase to enzymes of a similar scaffold or mechanism.Mechanistic and structural studies of the N-hydroxylating flavoprotein monooxygenases.Breaking a pathogen's iron will: Inhibiting siderophore production as an antimicrobial strategyRedesign of MST enzymes to target lyase activity instead promotes mutase and dehydratase activities.Holo Structure and Steady State Kinetics of the Thiazolinyl Imine Reductases for Siderophore Biosynthesis.Compensating for the absence of selenocysteine in high-molecular weight thioredoxin reductases: the electrophilic activation hypothesis.Ligand binding phenomena that pertain to the metabolic function of renalase.Biosynthesis of an Opine Metallophore by Pseudomonas aeruginosa.Nonribosomal peptides for iron acquisition: pyochelin biosynthesis as a case study.Unraveling the Structure and Mechanism of the MST(ery) EnzymesStaphylopine, pseudopaline, and yersinopine dehydrogenases: A structural and kinetic analysis of a new functional class of opine dehydrogenaseStuffed Methyltransferase Catalyzes the Penultimate Step of Pyochelin BiosynthesisStaphylopine and pseudopaline dehydrogenase from bacterial pathogens catalyze reversible reactions and produce stereospecific metallophoresPvdF of pyoverdin biosynthesis is a structurally unique N10-formyltetrahydrofolate-dependent formyltransferaseNot as easy as π: An insertional residue does not explain the π-helix gain-of-function in two-component FMN reductasesChanges in the allosteric site of human liver pyruvate kinase upon activator binding include the breakage of an intersubunit cation-π bond
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description
investigador
@es
researcher
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name
Audrey L Lamb
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type
label
Audrey L Lamb
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prefLabel
Audrey L Lamb
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P31
P496
0000-0002-2352-2130