Ligand-induced conformational changes in the capping subdomain of a bacterial old yellow enzyme homologue and conserved sequence fingerprints provide new insights into substrate binding.
about
A site-saturated mutagenesis study of pentaerythritol tetranitrate reductase reveals that residues 181 and 184 influence ligand binding, stereochemistry and reactivityThe Structure of Glycerol Trinitrate Reductase NerA fromAgrobacterium radiobacterReveals the Molecular Reason for Nitro- and Ene-Reductase Activity in OYE HomologuesHigh-resolution structures of cholesterol oxidase in the reduced state provide insights into redox stabilizationAn engineered old yellow enzyme that enables efficient synthesis of (4R,6R)-Actinol in a one-pot reduction systemComparative structural modeling of six old yellow enzymes (OYEs) from the necrotrophic fungus Ascochyta rabiei: insight into novel OYE classes with differences in cofactor binding, organization of active site residues and stereopreferencesIdentification of pOENI-1 and related plasmids in Oenococcus oeni strains performing the malolactic fermentation in wine.Structure and function of SET and MYND domain-containing proteins.Structural insights into the ene-reductase synthesis of profens.Redundancy of enzymes for formaldehyde detoxification in Pseudomonas putida.Towards structural studies of the old yellow enzyme homologue SYE4 from Shewanella oneidensis and its complexes at atomic resolution.Structural investigation into the C-terminal extension of the ene-reductase from Ralstonia (Cupriavidus) metallidurans.Structural dissection of Shewanella oneidensis old yellow enzyme 4 bound to a Meisenheimer complex and (nitro)phenolic ligands.The crystal structure of XdpB, the bacterial old yellow enzyme, in an FMN-free form.
P2860
Q27666872-34E1FF4C-7125-4F01-9B18-DB9300649474Q27677485-BE4F7BFD-6419-4958-AAF5-224F8B2CD0BCQ27696316-CDB8FA4A-3AD3-40CD-9272-48898FC67A9CQ27697686-DC2C187C-4CA6-44D6-87D6-DA9F05B25BD2Q28538270-FDE859B4-3A7A-4ADA-965F-1D486208DBF5Q34472187-2A20EE3C-DCE7-47F2-9251-EB053A52D553Q38314974-41903DA9-86EB-4E66-A456-C219387EEDC0Q38686111-7B260156-C0E4-445B-9B84-34FB7AF7ADF9Q42615686-4DC15FC9-1D44-4168-876F-2701650ACD6FQ42938676-9CC32FDD-281D-4F9F-A466-D97DAC0BF16BQ43032019-FC58A4CB-8257-4D3C-AAF9-187D30567BA5Q47719298-38501516-0FFD-48A5-BACB-4163D29D5F0BQ55434542-7D9F9AF7-B8C2-420A-A3CA-B93FAEB16199
P2860
Ligand-induced conformational changes in the capping subdomain of a bacterial old yellow enzyme homologue and conserved sequence fingerprints provide new insights into substrate binding.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Ligand-induced conformational ...... sights into substrate binding.
@en
Ligand-induced conformational ...... sights into substrate binding.
@nl
type
label
Ligand-induced conformational ...... sights into substrate binding.
@en
Ligand-induced conformational ...... sights into substrate binding.
@nl
prefLabel
Ligand-induced conformational ...... sights into substrate binding.
@en
Ligand-induced conformational ...... sights into substrate binding.
@nl
P2093
P2860
P356
P1476
Ligand-induced conformational ...... sights into substrate binding.
@en
P2093
Debbie van den Hemel
Jozef Van Beeumen
Savvas N Savvides
P2860
P304
28152-28161
P356
10.1074/JBC.M603946200
P407
P577
2006-07-20T00:00:00Z