Contribution of the active-site metal cation to the catalytic activity and to the conformational stability of phosphotriesterase: temperature- and pH-dependence.

Contribution of the active-site metal cation to the catalytic activity and to the conformational stability of phosphotriesterase: temperature- and pH-dependence.

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http://www.wikidata.org/entity/Q42284276
Structural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilusStructural and Enzymatic characterization of the lactonase SisLac from Sulfolobus islandicusLight-induced oxidative stress, N-formylkynurenine, and oxygenic photosynthesis.Evolutionary expansion of the amidohydrolase superfamily in bacteria in response to the synthetic compounds molinate and diuron.Mechanistic study of manganese-substituted glycerol dehydrogenase using a kinetic and thermodynamic analysis.Conformational variability of organophosphorus hydrolase upon soman and paraoxon binding.Molecular dynamics simulations of the detoxification of paraoxon catalyzed by phosphotriesterase.Organophosphorus hydrolase as an in vivo catalytic nerve agent bioscavenger.Update on biochemical properties of recombinant Pseudomonas diminuta phosphotriesterase.Anomalous scattering analysis of Agrobacterium radiobacter phosphotriesterase: the prominent role of iron in the heterobinuclear active site.New and highly active microbial phosphotriesterase sources.Immobilization of organophosphate hydrolase on an amyloid fibril nanoscaffold: towards bioremediation and chemical detoxification.The effect of conformational variability of phosphotriesterase upon N-acyl-L-homoserine lactone and paraoxon binding: insights from molecular dynamics studies.Substitution of the catalytic metal and protein PEGylation enhances activity and stability of bacterial phosphotriesterase.
P2860

Contribution of the active-site metal cation to the catalytic activity and to the conformational stability of phosphotriesterase: temperature- and pH-dependence.

Item
http://www.wikidata.org/entity/Q42284276
description
2004 nî lūn-bûn
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2004年の論文
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2004年論文
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2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
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name
Contribution of the active-sit ...... emperature- and pH-dependence.
@en
Contribution of the active-sit ...... emperature- and pH-dependence.
@nl
type
label
Contribution of the active-sit ...... emperature- and pH-dependence.
@en
Contribution of the active-sit ...... emperature- and pH-dependence.
@nl
prefLabel
Contribution of the active-sit ...... emperature- and pH-dependence.
@en
Contribution of the active-sit ...... emperature- and pH-dependence.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P932
P356
P1433
P1476
Contribution of the active-sit ...... temperature- and pH-dependence
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P932