about
Structure and mechanism of 3-deoxy-D-manno-octulosonate 8-phosphate synthaseStructures of Aquifex aeolicus KDO8P synthase in complex with R5P and PEP, and with a bisubstrate inhibitor: role of active site water in catalysisFunction of His185 in Aquifex aeolicus 3-deoxy-D-manno-octulosonate 8-phosphate synthaseStructure-based design of novel inhibitors of 3-deoxy-D-manno-octulosonate 8-phosphate synthaseThe Tail of KdsC: CONFORMATIONAL CHANGES CONTROL THE ACTIVITY OF A HALOACID DEHALOGENASE SUPERFAMILY PHOSPHATASECrystal structure of the reaction complex of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Thermotoga maritima refines the catalytic mechanism and indicates a new mechanism of allosteric regulation.Analysis of the arabinose-5-phosphate isomerase of Bacteroides fragilis provides insight into regulation of single-domain arabinose phosphate isomerases.Escherichia coli YrbI is 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase.Detoxifying Escherichia coli for endotoxin-free production of recombinant proteins.Unique biosynthesis of dehydroquinic acid?Probing the potential metal binding site in Escherichia coli 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (phenylalanine-sensitive).Identification and characterization of bacterial cutinase.Characterization of Escherichia coli D-arabinose 5-phosphate isomerase encoded by kpsF: implications for group 2 capsule biosynthesis.Bacillus subtilis 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase revisited: resolution of two long-standing enigmas.Escherichia coli YrbH is a D-arabinose 5-phosphate isomerase.A novel strategy for enhancing extracellular secretion of recombinant proteins in Escherichia coli.Arabinose 5-phosphate isomerase as a target for antibacterial design: studies with substrate analogues and inhibitors.A novel glucose 6-phosphate isomerase from Listeria monocytogenes.Conversion of aquifex aeolicus 3-deoxy-d-manno-octulosonate 8-phosphate synthase, a metalloenzyme, into a nonmetalloenzyme.Insights into the mechanism of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (Phe) from Escherichia coli using a transient kinetic analysis.New insights into the evolutionary links relating to the 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase subfamilies.Modification of lipopolysaccharide with colanic acid (M-antigen) repeats in Escherichia coli.Essential cysteines in 3-deoxy-D-manno-octulosonic acid 8-phosphate synthase from Escherichia coli: analysis by chemical modification and site-directed mutagenesis.Stereochemical course of the methylation of the polygalacturonic acid carboxyl groups of pectinOverproduction and one-step purification of Escherichia coli UDP-N-acetylglucosamine enolpyruvyl reductaseStereochemical course of the biosynthesis of 1-aminocyclopropane-1-carboxylic acid. I. Role of the asymmetric sulfonium pole and the alpha-amino acid centerPermeation of buprenorphine and its 3-alkyl-ester prodrugs through human skinIdentification of essential histidine residues in 3-deoxy-D-manno-octulosonic acid 8-phosphate synthase: analysis by chemical modification with diethyl pyrocarbonate and site-directed mutagenesisPreliminary X-ray analysis of a new crystal form of the Escherichia coli KDO8P synthaseA metal bridge between two enzyme families. 3-deoxy-D-manno-octulosonate-8-phosphate synthase from Aquifex aeolicus requires a divalent metal for activityNeisseria gonorrhoeae 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase does not catalyze the formation of the ribo analogueProbing the stereochemistry of E. coli 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (phenylalanine-sensitive)-catalyzed synthesis of KDO 8-P analoguesIsolation and Identification of Two l-Azetidine-2-carboxylic Acid-Degrading Soil Microorganisms, Enterobacter agglomerans and Enterobacter amnigenus
P50
Q27621861-D4F1D101-3AF0-41D8-98CD-B28A1017C412Q27636925-08DC4002-7211-429A-8DD8-CF7F2BFAC67BQ27639984-0DD16EA7-755E-4A81-81A7-5A562F861A48Q27642792-4F673E16-1DF2-4D66-BBA5-FA9B4AC0E575Q27657281-FAF18D50-3ECB-4980-8F7F-C812FEC4BEDDQ30434051-0065669F-E829-44AE-B9EA-F316AE38A6BCQ34056790-8C2DE464-47D3-44AF-B746-2348973717AFQ34183951-CD2E0EE0-60ED-41CC-AA46-C1B8CD570874Q35503548-28FFE66E-28C2-49F6-B5FD-DBF36ED0B82FQ35894237-DCBED392-C3B4-4775-8665-CFC5E8A63682Q38329600-CDC5EB55-2015-4B8A-846D-97A741E52D18Q40419589-A37F1CA9-3C8C-4F22-B66D-AE765910DBD5Q41772394-9CFA57AE-B7FB-41E4-9927-63695570DBBBQ41985742-017B3162-583F-4CE9-99D9-1FE91F148706Q42601558-14809E56-71F1-4E96-A50C-8FA0CFF078EAQ43761702-3EC6F796-BBA9-460B-BC93-3DDBD6DD9BC9Q43833813-57558A7E-A131-4A28-AC94-60A969167540Q44073972-9C79E9A6-8633-49A5-A594-69D5C92FABBCQ44937725-E4A97193-7369-417C-81EB-F7E5AD85AA49Q45028063-E4666A10-7979-4443-B440-2E3647B234BEQ46844169-44AD3E22-B674-4295-8F86-0711FBC41D1BQ54448386-7EA241AA-6176-40C7-A197-2711EC9D4DDCQ54585476-830DD26D-F518-4D00-AC52-29E1E4E7DBA4Q70784908-11B3ED2F-966E-4659-B765-59DFAC37912AQ71363661-B14E02B9-B377-4098-985C-A98601789709Q71384682-94EBF08D-C792-4EB2-8E0E-ADC45A6A4DBBQ71742023-B03C272A-4443-421F-ADA1-5D142EFEBB5DQ73205487-E21A531A-FCCB-4D65-9960-789DB8B1CFC4Q73599068-2E442990-6ED2-4122-BB44-BE6CF1F09D3CQ73794351-85AA048F-D247-4ED0-B1DC-B77A66E96AA7Q74109199-719B0F32-358C-4FF7-AA5A-3C89609ED2E9Q74316076-1E4A8B1F-063C-40A8-9EAF-AA3A8A1FA144Q74457261-EF35FBC1-C962-431B-A98E-0FD3B9C8EAE8
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Ronald W Woodard
@nl
Ronald W Woodard
@sl
Ronald W. Woodard
@en
Ronald W. Woodard
@es
type
label
Ronald W Woodard
@nl
Ronald W Woodard
@sl
Ronald W. Woodard
@en
Ronald W. Woodard
@es
prefLabel
Ronald W Woodard
@nl
Ronald W Woodard
@sl
Ronald W. Woodard
@en
Ronald W. Woodard
@es
P106
P1153
7004557173
P31
P496
0000-0002-7472-3653