about
The beta bulge: a common small unit of nonrepetitive protein structureThree-dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivityX-ray crystallographic investigation of substrate binding to carboxypeptidase A at subzero temperature3-Phosphonopropionic acids inhibit carboxypeptidase A as multisubstrate analogues or transition-state analoguesCatalysis of carboxypeptidase A: promoted-water versus nucleophilic pathways.Dynamical search for bis-penicillamine enkephalin conformations.Handedness of crossover connections in beta sheets.Unified picture of mechanisms of catalysis by carboxypeptidase A.Mechanism of action of carboxypeptidase A in ester hydrolysisThe reverse turn as a polypeptide conformation in globular proteins.Protein hydration dynamics in solution: a critical survey.Zinc environment and cis peptide bonds in carboxypeptidase A at 1.75-A resolution.Cocatalytic zinc motifs in enzyme catalysis.Genomic and transcriptomic evidence for scavenging of diverse organic compounds by widespread deep-sea archaea.Structure of potato inhibitor complex of carboxypeptidase A at 5.5-A resolutionStructure of an actively exchanging complex between carboxypeptidase A and a substrate analogue.Carboxypeptidase A mechanisms.Protein conformation from electron spin relaxation data.Molecular analysis of the Aedes aegypti carboxypeptidase gene family.Coupling between oxidation state and hydrogen bond conformation in heme proteins.Quantum mechanical/molecular mechanical and density functional theory studies of a prototypical zinc peptidase (carboxypeptidase A) suggest a general acid-general base mechanism.Evidence for the general base mechanism in carboxypeptidase A-catalyzed reactions: partitioning studies on nucleophiles and H2(18)O kinetic isotope effects.A proposed model for interaction of polypeptides with RNA.Complex between carboxypeptidase A and a hydrated ketomethylene substrate analogueCrystallographic studies on apocarboxypeptidase A and the complex with glycyl-L-tyrosine.Binding of a possible transition state analogue to the active site of carboxypeptidase A.Active-site zinc ligands and activated H2O of zinc enzymesA glutamate residue contributes to the exopeptidase specificity in aminopeptidase AThe pH-dependence and group modification of beta-lactamase I.Amino acid sequence of rabbit kidney neutral endopeptidase 24.11 (enkephalinase) deduced from a complementary DNA.Analysis of the code relating sequence to conformation in globular proteins. Development of a stereochemical alphabet on the basis of intra-residue information.Analysis of the code relating sequence to conformation in globular proteins. An informational analysis of the role of the residue in determining the conformation of its neighbours in the primary sequence.Mechanical deformation enhances catalytic activity of crystalline carboxypeptidase A.Metal-replacement studies in Bacillus stearothermophilus aldolase and a comparison of the mechanisms of class I and class II aldolases.Solvent accessibilities in glycyl, alanyl and seryl dipeptides.
P2860
Q24605097-3FA86A6B-F333-498A-8F98-6E43FC26D296Q27658102-205DAA41-E16C-41CC-809E-B80BD3374A50Q27728603-0298834F-6957-424C-AFC0-6FF7C62E33FAQ28362707-8EE70440-060A-427A-93F4-FD329B45F97BQ34059864-60BD1590-B2B1-4F36-86CC-1E83979B7292Q34088232-9C8F8EC2-A3BA-4188-B3CC-896B41FEBA78Q35015514-9DC8D8FB-AA51-4DE1-B37B-F55F50CB5D00Q35016603-A70314F3-B8AE-4B30-B207-0194B3BC338FQ35033601-AAA71CCD-98F2-4039-93EA-6A3B1A9EDC2DQ35096739-06DE3E65-70BD-4EAB-BD4F-57253C9514A1Q35214048-24C870A4-0B68-43AB-B2DB-BBFDB1A256EBQ35373992-70098AC2-F471-410D-8077-78E172C1E6E9Q36194705-743A3EA6-6F41-4593-8137-3D344BE1B551Q36320710-6A8B9406-549A-4D19-8560-A728410D8DBFQ36351553-7515CCD2-A71B-46C3-9AB4-40226FB3ECE0Q36392679-02A7C5AA-8F2E-4CC9-B833-2A575920AE68Q36396469-56D6CABD-EF85-4F27-83B7-96E139799666Q36596537-6FFC4BE3-E076-44B9-8378-54A3063C4A10Q37170566-46EF1DD9-DAFA-4177-8804-0C351F41E0B7Q37318986-59A0BD6D-6267-49EE-8C0C-4E126019D2BAQ37340639-F66B7BDF-E96A-4A6A-BC9E-BB398EF25BB0Q37343706-28D35524-6C31-4D82-A6E9-69F53664B247Q37429563-FE40F4CB-9AEE-4735-8077-A2C95F6668ACQ37484695-E594413E-02BE-4051-958A-06D8A5962668Q37508588-A4F17837-437F-499A-B21A-6CCB9DCC7C7EQ37535497-6B1A3DA1-CDBA-4F28-B0C2-4CED76157172Q37662485-107AF3ED-B839-4B4F-962D-B164B0AB0E1FQ38334093-7AA5135D-4350-435F-AC72-734CF5C9DB4AQ39066661-2F657E8E-B5E7-4D7B-937D-44ADD732FEF5Q41363012-D5A0E0B3-F8F1-4F09-B2BA-4FE9AB67FC11Q41854347-349467D8-E5C5-4996-826A-CF289BB287F5Q41908902-4D50CA27-EADE-420D-9A55-92947295DEE4Q42844622-852A4C05-2CFE-4B0D-8A92-F6D1643AFA12Q42916768-A683038E-83F9-4A10-BF36-1BE6CBE60790Q42932470-8924F8EA-3CDC-4297-997A-E416F41554E3
P2860
description
1971 nî lūn-bûn
@nan
1971年の論文
@ja
1971年学术文章
@wuu
1971年学术文章
@zh-cn
1971年学术文章
@zh-hans
1971年学术文章
@zh-my
1971年学术文章
@zh-sg
1971年學術文章
@yue
1971年學術文章
@zh
1971年學術文章
@zh-hant
name
Carboxypeptidase A: a protein and an enzyme.
@en
type
label
Carboxypeptidase A: a protein and an enzyme.
@en
prefLabel
Carboxypeptidase A: a protein and an enzyme.
@en
P1476
Carboxypeptidase A: a protein and an enzyme
@en
P2093
F A Quiocho
W N Lipscomb
P577
1971-01-01T00:00:00Z