about
Structure of the potato inhibitor complex of carboxypeptidase A at 2.5-A resolutionStructure, properties, and engineering of the major zinc binding site on human albuminStructure of aspartoacylase, the brain enzyme impaired in Canavan diseaseX-ray structure of ILL2, an auxin-conjugate amidohydrolase fromArabidopsis thalianaZinc environment and cis peptide bonds in carboxypeptidase A at 1.75-A resolution.A structural and functional analysis of Nna1 in Purkinje cell degeneration (pcd) mice.Binding of ligands to the active site of carboxypeptidase AQuantum mechanical/molecular mechanical and density functional theory studies of a prototypical zinc peptidase (carboxypeptidase A) suggest a general acid-general base mechanism.On the origin of the catalytic power of carboxypeptidase A and other metalloenzymes.Binding of a possible transition state analogue to the active site of carboxypeptidase A.Effects of pH on the structure and function of carboxypeptidase A: crystallographic studies.A survey of x-ray diffraction studies of enzyme-other molecule interactions as possible models for receptor sites.Sensitive luciferin derived probes for selective carboxypeptidase activity.Approaches to artificial enzymes.Tetrazole analogs of amino acids as constituents of modifiers of carboxypeptidase A catalysis.Predictive methods for computational metalloenzyme redesign - a test case with carboxypeptidase A.Three-dimensional structural resemblance between leucine aminopeptidase and carboxypeptidase A revealed by graph-theoretical techniques.
P2860
Q24611716-D53C53ED-DE07-4103-B387-E0539ED31395Q24658366-A77EDF96-C993-4447-A1FB-23F86AEA856FQ27640995-BB5731B8-672D-449C-95CE-5281B65FFEA7Q27650791-CB98BE00-2F19-4E39-B335-F30C627F1FCDQ35373992-0E21458A-E2FD-4C8E-B510-B209E0561C54Q36329799-25EE540F-B46D-4956-826E-4175D59B8564Q36367202-DC50C1D5-7ED5-4749-B841-F6CD86E74148Q37340639-1E72D207-0359-4A03-A312-9B4DD6BE95E5Q37399660-1A1BD9D8-50B2-40CF-A4A9-C910582AABEBQ37535497-DB21041F-95D7-4A0C-BEB9-255AEF8326DBQ37580142-F64D2BA9-EA36-4CDC-A599-A043ADE8D7B2Q40125541-B5AF8C13-DDCB-48DD-B15F-775E05705D19Q41769789-84739DF8-DA2D-476B-B38C-4849C61852CDQ43904652-53422A1B-57F9-4DE9-B4C4-BF3F78B3C732Q44582684-C84325FD-608C-47EF-BFC8-757A61269F8DQ46042058-D8EB985D-342B-47DC-85F8-6942B3542763Q52421069-3C16EE57-C03E-485F-9ED9-AC4129ECFE67
P2860
description
1980 nî lūn-bûn
@nan
1980年の論文
@ja
1980年学术文章
@wuu
1980年学术文章
@zh-cn
1980年学术文章
@zh-hans
1980年学术文章
@zh-my
1980年学术文章
@zh-sg
1980年學術文章
@yue
1980年學術文章
@zh
1980年學術文章
@zh-hant
name
Carboxypeptidase A mechanisms.
@ast
Carboxypeptidase A mechanisms.
@en
type
label
Carboxypeptidase A mechanisms.
@ast
Carboxypeptidase A mechanisms.
@en
prefLabel
Carboxypeptidase A mechanisms.
@ast
Carboxypeptidase A mechanisms.
@en
P2860
P356
P1476
Carboxypeptidase A mechanisms.
@en
P2093
W N Lipscomb
P2860
P304
P356
10.1073/PNAS.77.7.3875
P407
P577
1980-07-01T00:00:00Z