The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad
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Direct Ab-initio Molecular Dynamics (AIMD) Study on the Radiation Effects on Catalytic Triad composed of Ser-His-Glu residues
High energy irradiation to the hydrogen bonded system is important in relevance with the initial process of DNA and enzyme damages. In the present study, the effects of radiation to catalytic triad have been investigated by means of direct ab-initio molecular dynamics (AIMD) calculation. As a model of the catalytic triad, Ser-His-Glu residue, which is one of the important enzymes in the acylati...
متن کاملDirect Ab-Initio Molecular Dynamics Study on the Radiation Effects on Catalytic Triad Composed of Ser-His-Glu Residues
High energy irradiation to the hydrogen bonded system is important in relevance with the initial process of DNA and enzyme damages. In the present study, the effects of radiation to catalytic triad have been investigated by means of direct ab-initio molecular dynamics (AIMD) calculation. As a model of the catalytic triad, Ser-His-Glu residue, which is one of the important enzymes in the acylati...
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No. Haka7191 Beamline(s): X4A, X12C Introduction: Aspartyl dipeptidase (peptidase E) and tripeptidase (peptidase T) from Salmonella typhimurium are intracellular peptidases with very different specificities and structures. Aspartyl dipeptidase is a serine hydrolase that cleaves dipeptides with an N-terminal aspartate, and tripeptidase is a metallopeptidase that releases the N-terminal, preferab...
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LD-Carboxypeptidases (EC 3.4.17.13) are named for their ability to cleave amide bonds between l- and d-amino acids, which occur naturally in bacterial peptidoglycan. They are specific for the link between meso-diaminopimelic acid and d-alanine and therefore degrade GlcNAc-MurNAc tetrapeptides to the corresponding tripeptides. As only the tripeptides can be reused as peptidoglycan building block...
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Proteolytic processing of capsid assembly protein precursors by herpesvirus proteases is essential for virion maturation. A 2.5 A crystal structure of the human cytomegalovirus protease catalytic domain has been determined by X-ray diffraction. The structure defines a new class of serine protease with respect to global-fold topology and has a catalytic triad consisting of Ser-132, His-63, and H...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2000
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.260376797