A glutamate residue contributes to the exopeptidase specificity in aminopeptidase A
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Identification of human aminopeptidase O, a novel metalloprotease with structural similarity to aminopeptidase B and leukotriene A4 hydrolaseHuman leukocyte-derived arginine aminopeptidase. The third member of the oxytocinase subfamily of aminopeptidasesTma108, a putative M1 aminopeptidase, is a specific nascent chain-associated protein in Saccharomyces cerevisiae.Enzymatic properties of human aminopeptidase A. Regulation of its enzymatic activity by calcium and angiotensin IVAminopeptidase B, a glucagon-processing enzyme: site directed mutagenesis of the Zn2+-binding motif and molecular modellingStructural origins for the loss of catalytic activities of bifunctional human LTA4H revealed through molecular dynamics simulations.Placental leucine aminopeptidase- and aminopeptidase A- deficient mice offer insight concerning the mechanisms underlying preterm labor and preeclampsia.The role of multifunctional M1 metallopeptidases in cell cycle progressionStructure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active siteStructural basis for the inhibition of M1 family aminopeptidases by the natural product actinonin: Crystal structure in complex with E. coli aminopeptidase N.Role of angiotensin III in hypertension.Biochemical and enzymatic properties of the M1 family of aminopeptidases involved in the regulation of blood pressure.Structural and Functional Determinants of gamma-Secretase, an Intramembrane Protease Implicated in Alzheimer's Disease.Glu-333 of nicastrin directly participates in gamma-secretase activity.Histidine 379 of human laeverin/aminopeptidase Q, a nonconserved residue within the exopeptidase motif, defines its distinctive enzymatic propertiesGlu(332) in the Nicastrin ectodomain is essential for gamma-secretase complex maturation but not for its activity.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.Modulating the substrate specificity of LTA4H aminopeptidase by using chemical compounds and small-molecule-guided mutagenesis.Identification of threonine 348 as a residue involved in aminopeptidase A substrate specificity.The catalytic and protein-protein interaction domains are required for APM1 function.Contribution of molecular modeling and site-directed mutagenesis to the identification of two structural residues, Arg-220 and Asp-227, in aminopeptidase A.PepN, the major Suc-LLVY-AMC-hydrolyzing enzyme in Escherichia coli, displays functional similarity with downstream processing enzymes in Archaea and eukarya. Implications in cytosolic protein degradation.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.Leukotriene A4 hydrolase, insights into the molecular evolution by homology modeling and mutational analysis of enzyme from Saccharomyces cerevisiae.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 glutamate residue contributes to the exopeptidase specificity in aminopeptidase A
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh
1998年學術文章
@zh-hant
name
A glutamate residue contributes to the exopeptidase specificity in aminopeptidase A
@en
type
label
A glutamate residue contributes to the exopeptidase specificity in aminopeptidase A
@en
prefLabel
A glutamate residue contributes to the exopeptidase specificity in aminopeptidase A
@en
P2093
P2860
P356
P1433
P1476
A glutamate residue contributes to the exopeptidase specificity in aminopeptidase A
@en
P2093
P2860
P304
P356
10.1042/BJ3340407
P407
P478
334 ( Pt 2)
P50
P577
1998-09-01T00:00:00Z