Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes
about
A model of tripeptidyl-peptidase I (CLN2), a ubiquitous and highly conserved member of the sedolisin family of serine-carboxyl peptidasesIntrinsic evolutionary constraints on protease structure, enzyme acylation, and the identity of the catalytic triadThe catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active siteStructure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosisCrystal Structure and Autoactivation Pathway of the Precursor Form of Human Tripeptidyl-peptidase 1, the Enzyme Deficient in Late Infantile Ceroid LipofuscinosisUnconventional serine proteases: variations on the catalytic Ser/His/Asp triad configurationComparative modeling of CASP4 target proteins: combining results of sequence search with three-dimensional structure assessment.SMpred: a support vector machine approach to identify structural motifs in protein structure without using evolutionary information.The Bacillus subtilis signaling protein SpoIVB defines a new family of serine peptidasesCrystallographic and biochemical investigations of kumamolisin-As, a serine-carboxyl peptidase with collagenase activity.Determination of the substrate specificity of tripeptidyl-peptidase I using combinatorial peptide libraries and development of improved fluorogenic substrates.New families of carboxyl peptidases: serine-carboxyl peptidases and glutamic peptidases.The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum.The genetic spectrum of human neuronal ceroid-lipofuscinoses.Structure and function studies on enzymes with a catalytic carboxyl group(s): from ribonuclease T1 to carboxyl peptidasesCatalytic residues and substrate specificity of scytalidoglutamic peptidase, the first member of the eqolisin in family (G1) of peptidases.Clarification of the mechanism of acylation reaction and origin of substrate specificity of the serine-carboxyl peptidase sedolisin through QM/MM free energy simulationsThe intracellular location and function of proteins of neuronal ceroid lipofuscinoses.The importance of dynamics in substrate-assisted catalysis and specificity.The QM/MM molecular dynamics and free energy simulations of the acylation reaction catalyzed by the serine-carboxyl peptidase kumamolisin-As.Development of enzyme technology for Aspergillus oryzae, A. sojae, and A. luchuensis, the national microorganisms of Japan.N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I.Collagenolytic serine-carboxyl proteinase from Alicyclobacillus sendaiensis strain NTAP-1: purification, characterization, gene cloning, and heterologous expression.A tripeptidyl peptidase 1 is a binding partner of the Golgi pH regulator (GPHR) in Dictyostelium.Aorsin, a novel serine proteinase with trypsin-like specificity at acidic pH.The Physarum polycephalum php gene encodes a unique cold-adapted serine-carboxyl peptidase, physarolisin II.Maturation of human tripeptidyl-peptidase I in vitro.Ser475, Glu272, Asp276, Asp327, and Asp360 are involved in catalytic activity of human tripeptidyl-peptidase I.A new kumamolisin-like protease fromAlicyclobacillus acidocaldarius: an enzyme active under extreme acidic conditions
P2860
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P2860
Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes
description
2001 nî lūn-bûn
@nan
2001 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes
@ast
Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes
@en
Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes
@nl
type
label
Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes
@ast
Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes
@en
Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes
@nl
prefLabel
Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes
@ast
Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes
@en
Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes
@nl
P2093
P356
P1476
Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes
@en
P2093
A Gustchina
A Wlodawer
P2888
P356
10.1038/87610
P577
2001-05-01T00:00:00Z
P5875
P6179
1026112748