نتایج جستجو برای: contains a typical catalytic site of wcgpc

تعداد نتایج: 23295001  

Journal: :Acta crystallographica. Section F, Structural biology communications 2014
J Guo J B Cooper S P Wood

Endothiapepsin is a typical member of the aspartic proteinase family. The catalytic mechanism of this family is attributed to two conserved catalytic aspartate residues, which coordinate the hydrolysis of a peptide bond. An oligopeptide inhibitor (IC50 = 0.62 µM) based on a reduced-bond transition-state inhibitor of mucorpepsin was co-crystallized with endothiapepsin and the crystal structure o...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1995
J Guo W Huang G W Zhou R J Fletterick T S Scanlan

The variable-region peptide sequence and steady-state kinetic behavior are compared for a family of catalytic antibodies that arose from the same immune response to a transition-state analog. The crystal structure of the most catalytically active member of the family (17E8) has been solved to 2.5 A resolution and shows that the antibody active site contains a SerH99-HisH35 (H = heavy chain) cat...

Journal: :Journal of biochemistry and molecular biology 2007
Hyun-Sic Kim Ji-Man Kim Kyung-Baeg Roh Hyeon-Hwa Lee Su-Jin Kim Young Hee Shin Bok Luel Lee

An Asp/His catalytic site of 10-formyltetrahydrofolate dehydrogenase (FDH) was suggested to have a similar catalytic topology with the Asp/His catalytic site of serine proteases. Many studies supported the hypothesis that serine protease inhibitors can bind and modulate the activity of serine proteases by binding to the catalytic site of serine proteases. To explore the possibility that soybean...

2010
Nathalie Dautin

Serine Protease Autotransporters of Enterobacteriaceae (SPATEs) constitute a large family of proteases secreted by Escherichia coli and Shigella. SPATEs exhibit two distinct proteolytic activities. First, a C-terminal catalytic site triggers an intra-molecular cleavage that releases the N-terminal portion of these proteins in the extracellular medium. Second, the secreted N-terminal domains of ...

Journal: :Journal of molecular biology 2015
Sara M O'Rourke William Estell William G Scott

We report here that a single additional trans-Hoogsteen base-pairing interaction in the minimal hammerhead ribozyme transforms an RNA sequence possessing typically modest catalytic activity into one possessing greatly enhanced catalytic activity that is instead typical of full-length natural hammerhead RNAs that have additional extensive tertiary contact interactions. Formation of this addition...

2013
Ang Gao Gui-ying Mei Shun Liu Ping Wang Qun Tang Yan-ping Liu Hui Wen Xiao-min An Li-qun Zhang Xiao-xue Yan Dong-cai Liang

Many pathogenic bacteria that infect humans, animals and plants rely on a quorum-sensing (QS) system to produce virulence factors. N-Acyl homoserine lactones (AHLs) are the best-characterized cell-cell communication signals in QS. The concentration of AHL plays a key role in regulating the virulence-gene expression and essential biological functions of pathogenic bacteria. N-Acyl homoserine lac...

پایان نامه :وزارت علوم، تحقیقات و فناوری - دانشگاه صنعتی اصفهان 1371

the effect of the presence of perforations on he stresses of a plate is a problem which is of great interest in structural design and in the mathemattical theory of elasticity. among the many hole patterns that are likely to require consideration is the ring of equally spaced circular holes. the present worke investigates stress & strain analysis of a thin isotropic circular plate containing a ...

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Neolithic period, the time when human start to change its way of life from hunting and gathering to framing and herding, is one of the most noticed cultural phenomenon by archaeologists. Kashan area is one of those regions that contains the oldest traces of this phenomenon, hence archaeological activities in the area goes back very early in Iran. Besides Sialk, that is most famous archaeologica...

2014
Yasumitsu Sakamoto Yoshiyuki Suzuki Ippei Iizuka Chika Tateoka Saori Roppongi Mayu Fujimoto Koji Inaka Hiroaki Tanaka Mika Masaki Kazunori Ohta Hirofumi Okada Takamasa Nonaka Yasushi Morikawa Kazuo T. Nakamura Wataru Ogasawara Nobutada Tanaka

The dipeptidyl aminopeptidase BII (DAP BII) belongs to a serine peptidase family, S46. The amino acid sequence of the catalytic unit of DAP BII exhibits significant similarity to those of clan PA endopeptidases, such as chymotrypsin. However, the molecular mechanism of the exopeptidase activity of family S46 peptidase is unknown. Here, we report crystal structures of DAP BII. DAP BII contains a...

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