The origin of the electrostatic perturbation in acetoacetate decarboxylase
about
Structural classification of proteins and structural genomics: new insights into protein folding and evolutionPhysicochemical Properties of Ion Pairs of Biological MacromoleculesProton transfer reactions and hydrogen-bond networks in protein environmentsDirect Observation of an Enamine Intermediate in Amine CatalysisStructure of the Bifunctional Acyltransferase/Decarboxylase LnmK from the Leinamycin Biosynthetic Pathway Revealing Novel Activity for a Double-Hot-Dog FoldStructural and Functional Characterization of MppR, an Enduracididine Biosynthetic Enzyme from Streptomyces hygroscopicus : Functional Diversity in the Acetoacetate Decarboxylase-like SuperfamilyStructure of the effector-binding domain of deoxyribonucleoside regulator DeoR from Bacillus subtilisCrystal structures and kinetics of Type III 3-phosphoglycerate dehydrogenase reveal catalysis by lysineElucidation of the bicarbonate binding site and insights into the carboxylation mechanism of (N(5))-carboxyaminoimidazole ribonucleotide synthase (PurK) from Bacillus anthracisDe-DUFing the DUFs: Deciphering distant evolutionary relationships of Domains of Unknown Function using sensitive homology detection methods.A thiolate anion buried within the hydrocarbon ruler perturbs PagP lipid acyl chain selectionOrigins of catalysis by computationally designed retroaldolase enzymes.Large shifts in pKa values of lysine residues buried inside a protein.Reaction of cis-3-chloroacrylic acid dehalogenase with an allene substrate, 2,3-butadienoate: hydration via an enamine.DNA as a versatile chemical component for catalysis, encoding, and stereocontrolConformational consequences of ionization of Lys, Asp, and Glu buried at position 66 in staphylococcal nucleaseProbing the chemical mechanism of saccharopine reductase from Saccharomyces cerevisiae using site-directed mutagenesis.Reactions of Cg10062, a cis-3-Chloroacrylic Acid Dehalogenase Homologue, with Acetylene and Allene Substrates: Evidence for a Hydration-Dependent Decarboxylation.Breaking the carboxyl rule: lysine 96 facilitates reprotonation of the Schiff base in the photocycle of a retinal protein from Exiguobacterium sibiricum.Arginine as a general acid catalyst in serine recombinase-mediated DNA cleavageMechanism of formate-nitrite transporters by dielectric shift of substrate acidity.Mathematical modelling of clostridial acetone-butanol-ethanol fermentation.Integrative modelling of pH-dependent enzyme activity and transcriptomic regulation of the acetone-butanol-ethanol fermentation of Clostridium acetobutylicum in continuous culture.Origin of the pKa shift of the catalytic lysine in acetoacetate decarboxylase.An extracellular ion pathway plays a central role in the cooperative gating of a K(2P) K+ channel by extracellular pH.A shift in the dominant phenotype governs the pH-induced metabolic switch of Clostridium acetobutylicumin phosphate-limited continuous cultures.Lysine relay mechanism coordinates intermediate transfer in vitamin B6 biosynthesis.Conversion of levulinic acid to 2-butanone by acetoacetate decarboxylase from Clostridium acetobutylicum.Benchmarking pKa prediction methods for Lys115 in acetoacetate decarboxylase.Coenzyme A-transferase-independent butyrate re-assimilation in Clostridium acetobutylicum-evidence from a mathematical model.
P2860
Q24632298-17B85209-52DF-48A9-8031-3346710B4185Q26782002-E7877C50-A52F-436E-8C32-F568AA2689BFQ27006718-0CFD84EC-DAD7-49CC-A003-6DEAB69C8F3EQ27658492-30201F62-67B5-4444-ABE0-EBA636B067FEQ27675905-3980098A-3D7B-4AA2-902B-DA80C969617AQ27678584-65E3CB7B-DEDD-44EC-8E55-A44D02ED64F0Q27690323-03B61458-5184-4FF6-8C1F-EBE866F52058Q27695692-47C10EC8-89C1-488A-9493-BF60E7BF77F7Q27696151-E895142E-63C0-4B46-84D9-F6615B310FE6Q28546880-B868B752-1D4B-4BA6-BD12-275653EF0D29Q28828313-D44036D9-98F5-4769-AF67-6E93DE758CC4Q33740304-B8739BD6-7A77-4F7C-8A8B-44981FDCCED4Q34750136-5C0D78DE-9480-438D-A8FF-4BE14149DB53Q35670316-414E1678-33C7-4011-BCA2-70FCD44C05B6Q35710979-F57D0B9A-6EC7-4136-AA91-4BF15F4CB742Q36026093-C46E2491-3D37-41CF-93B8-03F88B86B3FCQ36131254-7AA6A527-A47C-4FCF-9E9A-8CE2C67809B2Q36207492-9B627FF3-DBE7-4A8B-93DE-0FEBA11B17F4Q37175176-44D1BE4F-AAF7-4161-ADA9-18B01C32B741Q37213956-B025D251-0235-4FAD-8B4B-E0EC10C1704CQ38934953-6C616BDA-9B6F-40B6-8AF0-E2B15E892380Q39140219-80AA47D5-AD01-409D-BBDA-0D6741FEE2ADQ39482629-18DFFDE9-3B99-4D7F-B585-017629E4AFB2Q42973954-16E09EB4-6B52-4D4E-8232-7460FD5A7187Q43240562-12106A58-8C35-435F-AABA-A727C307DC52Q45332238-30728FC5-9BFC-408F-839E-2B0CF9FEFB54Q46019013-853CE559-70F4-4EB4-8E00-A6F84F468FD0Q46293215-DE52195A-AF2E-42D8-8299-8BDBC68A4EC4Q46389193-ED35123F-8A6B-4F57-9166-676052CF4148Q51051456-4BA8FB1F-13C0-417C-8DDD-FE86CD4C9F91
P2860
The origin of the electrostatic perturbation in acetoacetate decarboxylase
description
2009 nî lūn-bûn
@nan
2009 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
The origin of the electrostatic perturbation in acetoacetate decarboxylase
@ast
The origin of the electrostatic perturbation in acetoacetate decarboxylase
@en
The origin of the electrostatic perturbation in acetoacetate decarboxylase
@nl
type
label
The origin of the electrostatic perturbation in acetoacetate decarboxylase
@ast
The origin of the electrostatic perturbation in acetoacetate decarboxylase
@en
The origin of the electrostatic perturbation in acetoacetate decarboxylase
@nl
prefLabel
The origin of the electrostatic perturbation in acetoacetate decarboxylase
@ast
The origin of the electrostatic perturbation in acetoacetate decarboxylase
@en
The origin of the electrostatic perturbation in acetoacetate decarboxylase
@nl
P356
P1433
P1476
The origin of the electrostatic perturbation in acetoacetate decarboxylase
@en
P2093
Hiro Tsuruta
Meng-Chiao Ho
P2888
P356
10.1038/NATURE07938
P407
P577
2009-05-21T00:00:00Z
P5875
P6179
1018627042