Results 161 to 170 of about 25,546 (199)

Photoreactivity of histidyl residues in subtilisins Novo and DY. Photooxidation of subtilisins

International Journal of Peptide and Protein Research, 1987
Subtilisins Novo and DY were photoinactivated in the presence of methylene blue according to first order kinetics. The competitive inhibitor Nα‐benzoyl‐L‐arginine protected significantly against inactivation. Under the conditions employed in this study a selective photooxidation of the active site histidine 64 was achieved. Rate constants of 0.32 times
N, Genov, K, Idakieva
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Kinetic studies on the binding of Streptomyces subtilisin inhibitor with subtilisin BPN′

Archives of Biochemistry and Biophysics, 1980
Abstract The binding mechanism of Streptomyces subtilisin inhibitor and subtilisin BPN′ was studied kinetically with the stopped-flow method by monitoring the protein fluorescence increase due to complex formation. In the lower concentration range of proteins, the reaction followed the second-order kinetics.
Y, Uehara, B, Tonomura, K, Hiromi
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Protein engineering of subtilisin

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000
The serine protease subtilisin is an important industrial enzyme as well as a model for understanding the enormous rate enhancements affected by enzymes. For these reasons along with the timely cloning of the gene, ease of expression and purification and availability of atomic resolution structures, subtilisin became a model system for protein ...
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SUBTILISIN: AN ENZYME DESIGNED TO BE ENGINEERED

Trends in Biochemical Sciences, 1988
Abstract Almost every property of subtilisin, a simple bacterial serine protease, has been altered by protein engineering including its catalysis, substrate specificity, pH/rate profile, and stability to oxidative, thermal and alkaline inactivation.
J A, Wells, D A, Estell
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Alkaline-Resistance Model of Subtilisin ALP I, a Novel Alkaline Subtilisin

Journal of Biochemistry, 2001
The alkaline-resistance mechanism of the alkaline-stable enzymes is not yet known. To clarify the mechanism of alkaline-resistance of alkaline subtilisin, structural changes of two typical subtilisins, subtilisin ALP I (ALP I) and subtilisin Sendai (Sendai), were studied by means of physicochemical methods.
H, Maeda, O, Mizutani, Y, Yamagata, E, Ichishima, T, Nakajima   +4 more
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Crystal structures of Streptomyces subtilisin inhibitor and its complex with subtilisin BPN′

Nature, 1979
Crystal structure of a microbial protein proteinase inhibitor SSI (Streptomyces subtilisin inhibitor) and its complex with subtilisin BPN′ were solved at 2.6 A and 4.3 A resolution respectively. The mode of binding to the proteinase of SSI is compared with that of bovine pancreatic trypsin inhibitor, soybean trypsin inhibitor and the substrates ...
Y, Mitsui, Y, Satow, Y, Watanabe, S, Hirono, Y, Iitaka   +4 more
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Degradation of ribonuclease by subtilisin

Biochimica et Biophysica Acta, 1955
S M, KALMAN, K, LINDERSTRØM-LANG, M, OTTESEN, F M, RICHARDS   +3 more
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Plant subtilisins.

Biochemistry. Biokhimiia, 1999
This review presents a systematization of available data on subtilisin-like serine proteinases of plants. Enzymatic and physicochemical properties of the enzymes, their structure and processing, as well as their biological functions and origin are considered.
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The activation of chymotrypsinogen by subtilisin

Biochimica et Biophysica Acta, 1956
A, BRONFENBRENNER, K, LINDERSTROMLANG, M, OTTESEN   +2 more
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Versatility of subtilisin: A review on structure, characteristics, and applications

Biotechnology and Applied Biochemistry, 2022
Nur Aliyah Mohd Azrin, Mohd Shukuri Mohamad Ali, Raja Noor Zaliha Raja Abd Rahman   +2 more
exaly