Crystal Structure of D-Hydantoinase from Burkholderia pickettii at a Resolution of 2.7 Angstroms: Insights into the Molecular Basis of Enzyme Thermostability

Crystal Structure of D-Hydantoinase from Burkholderia pickettii at a Resolution of 2.7 Angstroms: Insights into the Molecular Basis of Enzyme Thermostability

Item
http://www.wikidata.org/entity/Q27641581
Structural bases for CRMP function in plexin-dependent semaphorin3A signalingThe functional role of the binuclear metal center in D-aminoacylase: one-metal activation and second-metal attenuationReversible Post-Translational Carboxylation Modulates the Enzymatic Activity of N -Acetyl- l -ornithine TranscarbamylaseThe mononuclear metal center of type-I dihydroorotase from aquifex aeolicusProteome adaptation to high temperatures in the ectothermic hydrothermal vent Pompeii wormIdentification of the Final Two Genes Functioning in Methanofuran Biosynthesis in Methanocaldococcus jannaschii.Divergent functions through alternative splicing: the Drosophila CRMP gene in pyrimidine metabolism, brain, and behavior.From sequence and structure of sulfotransferases and dihydropyrimidinases to an understanding of their mechanisms of action and function.Crystallization and preliminary crystallographic studies of the recombinant dihydropyrimidinase from Sinorhizobium meliloti CECT4114.Toward a cell-free hydantoinase process: screening for expression optimization and one-step purification as well as immobilization of hydantoinase and carbamoylase.Crystallization and X-ray diffraction analysis of dihydropyrimidinase from Saccharomyces kluyveri.Biochemical characterization of allantoinase from Escherichia coli BL21.The crystal structures of dihydropyrimidinases reaffirm the close relationship between cyclic amidohydrolases and explain their substrate specificity.Chemical rescue of the post-translationally carboxylated lysine mutant of allantoinase and dihydroorotase by metal ions and short-chain carboxylic acids.Activation of Latent Dihydroorotase from Aquifex aeolicus by Pressure.
P2860

Crystal Structure of D-Hydantoinase from Burkholderia pickettii at a Resolution of 2.7 Angstroms: Insights into the Molecular Basis of Enzyme Thermostability

Item
http://www.wikidata.org/entity/Q27641581
description
2003 nî lūn-bûn
@nan
2003 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Crystal Structure of D-Hydanto ...... asis of Enzyme Thermostability
@ast
Crystal Structure of D-Hydanto ...... asis of Enzyme Thermostability
@en
Crystal Structure of D-Hydanto ...... asis of Enzyme Thermostability
@nl
type
label
Crystal Structure of D-Hydanto ...... asis of Enzyme Thermostability
@ast
Crystal Structure of D-Hydanto ...... asis of Enzyme Thermostability
@en
Crystal Structure of D-Hydanto ...... asis of Enzyme Thermostability
@nl
prefLabel
Crystal Structure of D-Hydanto ...... asis of Enzyme Thermostability
@ast
Crystal Structure of D-Hydanto ...... asis of Enzyme Thermostability
@en
Crystal Structure of D-Hydanto ...... asis of Enzyme Thermostability
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P921
P932
P356
P1433
P1476
Crystal Structure of D-Hydanto ...... asis of Enzyme Thermostability
@en
P2093
P2860
P304
P31
P356
10.1128/JB.185.14.4038-4049.2003
P407
P433
P478
P50
P577
P698
P921
P932