نتایج جستجو برای: uncompetitive inhibitor

تعداد نتایج: 211497  

Journal: :The Biochemical journal 1990
S Zepeda O Monasterio T Ureta

An NADP(+)-dependent D-xylose dehydrogenase from pig liver cytosol was purified about 2000-fold to apparent homogeneity with a yield of 15% and specific activity of 6 units/mg of protein. An Mr value of 62,000 was obtained by gel filtration. PAGE in the presence of SDS gave an Mr value of 32,000, suggesting that the native enzyme is a dimer of similar or identical subunits. D-Xylose, D-ribose, ...

Journal: :The Journal of antibiotics 1997
N Nonaka Y Asai M Nishio K Takahashi T Okuda S Tanaka T Sugita T Ohnuki S Komatsubara

TMC-2A(1), -2B (2) and -2C (3), novel dipeptidyl peptidase IV (DPIV) inhibitors, were isolated from the fermentation broth of Aspergillus oryzae A374. TMC-2A, -2B and -2C inhibited rat kidney DPIV with IC50 value of 8.1 microM, 17 microM, and 20 microM, respectively, as well as human DPIV prepared from mononuclear cells and adenocarcinoma cells. TMC-2 compounds inhibited only DPIV among the pro...

Journal: :Bioscience, biotechnology, and biochemistry 2012
Eisuke Kato Kenichi Oikawa Keisuke Takahashi Jun Kawabata

2-Aminoresorcinol is a potent and selective intestinal glucosidase inhibitor. Unlike the majority of glucosidase inhibitors, it shows an uncompetitive mode of inhibition. In this study, we tested the intestinal glucosidase inhibitory activity of various 2-aminoresorcinol derivatives. We found that structural changes, in amino and two phenolic hydroxyl groups had a negative impact on inhibitory ...

Journal: :Biochemistry 2000
S L Parikh G Xiao P J Tonge

Structural and genetic studies indicate that the antibacterial compound triclosan, an additive in many personal care products, is an inhibitor of EnvM, the enoyl reductase from Escherichia coli. Here we show that triclosan specifically inhibits InhA, the enoyl reductase from Mycobacterium tuberculosis and a target for the antitubercular drug isoniazid. Binding of triclosan to wild-type InhA is ...

2002

Simultaneous exposure to a mixture can cause two or more chemicals to compete for enzyme-mediated biotransformation, resulting in an inhibition of at least one of the chemicals. The inhibition is termed ‘competitive’ when the chemicals compete as substrates for the same site on an enzyme. In ‘noncompetitive inhibition’, the inhibitor binds to the enzyme, causing a change in the stereochemical a...

Journal: :The Journal of biological chemistry 1977
T S Soper W M Jones B Lerner M Trop J M Manning

Purified D-amino acid transaminase from Bacillus sphaericus catalyzes an alpha,beta elimination from the D isomer of beta-chloroalanine to yield equivalent amounts of pyruvate, chloride, and ammonia; the L isomer of chloroalanine is not a substrate for this transaminase. During the beta elimination there is a synchronous loss in enzyme activity; the Kinact for beta-chloroalanine was estimated t...

2017
Stephanie M Stanford Alexander E Aleshin Vida Zhang Robert J Ardecky Michael P Hedrick Jiwen Zou Santhi R Ganji Matthew R Bliss Fusayo Yamamoto Andrey A Bobkov Janna Kiselar Yingge Liu Gregory W Cadwell Shilpi Khare Jinghua Yu Antonio Barquilla Thomas D Y Chung Tomas Mustelin Simon Schenk Laurie A Bankston Robert C Liddington Anthony B Pinkerton Nunzio Bottini

Obesity-associated insulin resistance plays a central role in type 2 diabetes. As such, tyrosine phosphatases that dephosphorylate the insulin receptor (IR) are potential therapeutic targets. The low-molecular-weight protein tyrosine phosphatase (LMPTP) is a proposed IR phosphatase, yet its role in insulin signaling in vivo has not been defined. Here we show that global and liver-specific LMPTP...

Journal: :ChemMedChem 2012
Sanjay Samanta Taian Cui Yulin Lam

West Nile virus (WNV), a member of the Flaviviridae family, is a mosquito-borne pathogen that causes a great number of human infections each year. Neither vaccines nor antiviral therapies are currently available for human use. In this study, a WNV NS2B-NS3 protease inhibitor with a 9,10-dihydro-3H,4aH-1,3,9,10a-tetraazaphenanthren-4-one scaffold was identified by screening a small library of no...

Journal: :The Journal of biological chemistry 1980
J R Farley J L Ivey D J Baylink

The skeletal isoenzyme of human alkaline phosphatase was partially purified from the serum of a patient with Paget’s disease. The pH dependence of the reaction with p-nitrophenyl phosphate (PNPP) suggests that either the reaction mechanism involves 2 dissociable residues on the enzyme (8.75 > pK1 > 8.2; 9.35 > pKz > 8.75), or that the monoanion is the active form of the phosphoryl substrate. In...

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