Support for a three-dimensional structure predicting a Cys-Glu-Lys catalytic triad for Pseudomonas aeruginosa amidase comes from site-directed mutagenesis and mutations altering substrate specificity.

Support for a three-dimensional structure predicting a Cys-Glu-Lys catalytic triad for Pseudomonas aeruginosa amidase comes from site-directed mutagenesis and mutations altering substrate specificity.

Item
http://www.wikidata.org/entity/Q41899389
Structural insights into the catalytic active site and activity of human Nit2/ω-amidase: kinetic assay and molecular dynamics simulationStructure of amidase from Pseudomonas aeruginosa showing a trapped acyl transfer reaction intermediate stateFunctional Proteomic and Structural Insights into Molecular Recognition in the Nitrilase Family Enzymes † ‡Identification of recurring protein structure microenvironments and discovery of novel functional sites around CYS residuesCrystallization, diffraction data collection and preliminary crystallographic analysis of hexagonal crystals of Pseudomonas aeruginosa amidase.Nitrilase enzymes and their role in plant-microbe interactionsThe quaternary structure of the amidase from Geobacillus pallidus RAPc8 is revealed by its crystal packing.Nitrilase and its application as a 'green' catalyst.Nitrile-converting enzymes: an eco-friendly tool for industrial biocatalysis.Identification of essential residues in apolipoprotein N-acyl transferase, a member of the CN hydrolase family.Purification and characterization of a thermostable aliphatic amidase from the hyperthermophilic archaeon Pyrococcus yayanosii CH1.Bench scale production of benzohydroxamic acid using acyl transfer activity of amidase from Alcaligenes sp. MTCC 10674.Aliphatic amidase from Rhodococcus rhodochrous M8 is related to the nitrilase/cyanide hydratase family.Identification and characterization of a thermostable and cobalt-dependent amidase from Burkholderia phytofirmans ZJB-15079 for efficient synthesis of (R)-3,3,3-trifluoro-2-hydroxy-2-methylpropionic acid.Monoclonal antibodies recognize conformational epitopes on wild-type and recombinant mutant amidases from pseudomonas aeruginosa.Biochemical characterization of MelJ and MelK.
P2860

Support for a three-dimensional structure predicting a Cys-Glu-Lys catalytic triad for Pseudomonas aeruginosa amidase comes from site-directed mutagenesis and mutations altering substrate specificity.

Item
http://www.wikidata.org/entity/Q41899389
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
2002年论文
@zh
2002年论文
@zh-cn
name
Support for a three-dimensiona ...... ltering substrate specificity.
@en
type
label
Support for a three-dimensiona ...... ltering substrate specificity.
@en
prefLabel
Support for a three-dimensiona ...... ltering substrate specificity.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P932
P356
P1433
P1476
Support for a three-dimensiona ...... ltering substrate specificity.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P932