Common-type acylphosphatase: steady-state kinetics and leaving-group dependence
about
Biological phosphoryl-transfer reactions: understanding mechanism and catalysisAlkaline phosphatase mono- and diesterase reactions: comparative transition state analysisA Rigidifying Salt-Bridge Favors the Activity of Thermophilic Enzyme at High Temperatures at the Expense of Low-Temperature ActivityA nucleophilic catalysis step is involved in the hydrolysis of aryl phosphate monoesters by human CT acylphosphatasePduL is an evolutionarily distinct phosphotransacylase involved in B12-dependent 1,2-propanediol degradation by Salmonella enterica serovar typhimurium LT2.Acylphosphatase possesses nucleoside triphosphatase and nucleoside diphosphatase activities.
P2860
Common-type acylphosphatase: steady-state kinetics and leaving-group dependence
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Common-type acylphosphatase: steady-state kinetics and leaving-group dependence
@en
type
label
Common-type acylphosphatase: steady-state kinetics and leaving-group dependence
@en
prefLabel
Common-type acylphosphatase: steady-state kinetics and leaving-group dependence
@en
P2093
P2860
P356
P1433
P1476
Common-type acylphosphatase: steady-state kinetics and leaving-group dependence
@en
P2093
Pieraccini G
P2860
P304
P356
10.1042/BJ3270177
P407
P478
327 ( Pt 1)
P577
1997-10-01T00:00:00Z