A tyrosine residue essential for catalytic activity in aminopeptidase A.
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Fundamental challenges in mechanistic enzymology: progress toward understanding the rate enhancements of enzymesMolecular characterization of a puromycin-insensitive leucyl-specific aminopeptidase, PILS-APPurification and functional characterisation of rhiminopeptidase A, a novel aminopeptidase from the venom of Bitis gabonica rhinoceros.The closed structure of presequence protease PreP forms a unique 10,000 Angstroms3 chamber for proteolysis.Role of angiotensin III in hypertension.Biochemical and enzymatic properties of the M1 family of aminopeptidases involved in the regulation of blood pressure.Histidine 379 of human laeverin/aminopeptidase Q, a nonconserved residue within the exopeptidase motif, defines its distinctive enzymatic propertiesA glutamate residue contributes to the exopeptidase specificity in aminopeptidase ADeficiency of the Angiotensinase Aminopeptidase A Increases Susceptibility to Glomerular Injury.Exploration of Sitagliptin as a potential inhibitor for the M1 Alanine aminopeptidase enzyme in Plasmodium falciparum using computational docking.Involvement of arginine 878 together with Ca2+ in mouse aminopeptidase A substrate specificity for N-terminal acidic amino-acid residuesThe C-terminal domain, but not the interchain disulphide, is required for the activity and intracellular trafficking of aminopeptidase A.Identification of threonine 348 as a residue involved in aminopeptidase A substrate specificity.Contribution of molecular modeling and site-directed mutagenesis to the identification of two structural residues, Arg-220 and Asp-227, in aminopeptidase A.The C-terminal domain of aminopeptidase A is an intramolecular chaperone required for the correct folding, cell surface expression, and activity of this monozinc aminopeptidase.Human brain aminopeptidase A: biochemical properties and distribution in brain nuclei.Asparatic acid 221 is critical in the calcium-induced modulation of the enzymatic activity of human aminopeptidase A.
P2860
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P2860
A tyrosine residue essential for catalytic activity in aminopeptidase A.
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
A tyrosine residue essential for catalytic activity in aminopeptidase A.
@en
A tyrosine residue essential for catalytic activity in aminopeptidase A.
@nl
type
label
A tyrosine residue essential for catalytic activity in aminopeptidase A.
@en
A tyrosine residue essential for catalytic activity in aminopeptidase A.
@nl
prefLabel
A tyrosine residue essential for catalytic activity in aminopeptidase A.
@en
A tyrosine residue essential for catalytic activity in aminopeptidase A.
@nl
P2093
P2860
P356
P1433
P1476
A tyrosine residue essential for catalytic activity in aminopeptidase A
@en
P2093
P2860
P304
P356
10.1042/BJ3270883
P407
P478
327 ( Pt 3)
P50
P577
1997-11-01T00:00:00Z