pH-dependent structural changes in the active site of p-hydroxybenzoate hydroxylase point to the importance of proton and water movements during catalysis
about
BluB cannibalizes flavin to form the lower ligand of vitamin B12Structure and mechanism of ORF36, an amino sugar oxidizing enzyme in everninomicin biosynthesis .4-Hydroxybenzoate hydroxylase from Pseudomonas sp. CBS3. Purification, characterization, gene cloning, sequence analysis and assignment of structural features determining the coenzyme specificityHow pH Modulates the Reactivity and Selectivity of a Siderophore-Associated Flavin MonooxygenaseMechanism of Rifampicin Inactivation in Nocardia farcinicaAvoidable errors in deposited macromolecular structures: an impediment to efficient data mining.A molecular dynamics study in explicit water of the reduced and oxidized forms of yeast iso-1-cytochrome c--solvation and dynamic properties of the two oxidation states.In vivo investigation of the roles of FdmM and FdmM1 in fredericamycin biosynthesis unveiling a new family of oxygenases.Form follows function: structural and catalytic variation in the class a flavoprotein monooxygenases.Expression, purification, crystallization and initial crystallographic characterization of the p-hydroxybenzoate hydroxylase from Corynebacterium glutamicumEnergy Landscape Topography Reveals the Underlying Link Between Binding Specificity and Activity of EnzymesBiography of Martha L. LudwigSimilarity search for local protein structures at atomic resolution by exploiting a database management system.Hydroxylation of indole by laboratory-evolved 2-hydroxybiphenyl 3-monooxygenase.Rational engineering of p-hydroxybenzoate hydroxylase to enable efficient gallic acid synthesis via a novel artificial biosynthetic pathway.
P2860
Q24646824-7CBBFDD9-D481-4E08-8E0C-CD3F7C57FAC6Q27664658-F52D252B-FD46-4972-BFC6-BD172B7ADC23Q28284814-EE3A79E3-CDDA-462E-BB88-EC8C5E60498BQ28468160-3051508B-8423-430E-8C78-13A968A42352Q28554510-32BC6F06-318A-4429-83CD-9BD722144ADFQ30411764-A12802A3-DD86-4389-9E90-44BC329B6FA8Q32184449-709E506E-DE02-4100-ABCD-48195E99B8BAQ33484555-8B316018-712D-4338-A94D-BDB07C140606Q36538270-599CE9C0-E364-45F5-81E3-6E72697CD897Q36588510-493638CC-2CBF-43E8-A54C-BB0EFADC660EQ37000373-F4021976-140C-48B9-B551-02DAE724D52EQ37094475-B29CCC64-49AA-4B86-81D7-3F823917908DQ39178892-9BCFF89A-EF21-448B-B762-6A463B62982AQ44053784-28E9F659-E9B6-4712-AF17-8024D7659DE2Q47986891-A50F9B62-F72F-465C-9590-D6D2E1ECF5E9
P2860
pH-dependent structural changes in the active site of p-hydroxybenzoate hydroxylase point to the importance of proton and water movements during catalysis
description
1996 nî lūn-bûn
@nan
1996 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
pH-dependent structural change ...... ter movements during catalysis
@ast
pH-dependent structural change ...... ter movements during catalysis
@en
pH-dependent structural change ...... ter movements during catalysis
@nl
type
label
pH-dependent structural change ...... ter movements during catalysis
@ast
pH-dependent structural change ...... ter movements during catalysis
@en
pH-dependent structural change ...... ter movements during catalysis
@nl
prefLabel
pH-dependent structural change ...... ter movements during catalysis
@ast
pH-dependent structural change ...... ter movements during catalysis
@en
pH-dependent structural change ...... ter movements during catalysis
@nl
P2093
P3181
P356
P1433
P1476
pH-dependent structural change ...... ter movements during catalysis
@en
P2093
P304
P3181
P356
10.1021/BI951344I
P407
P577
1996-01-16T00:00:00Z