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His345 mutant of angiotensin-converting enzyme 2 (ACE2) remains enzymatically active against angiotensin II.
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Feinberg Cardiovascular and Renal Research Institute, Department of Medicine-Nephrology and Hypertension, Northwestern University Feinberg School of Medicine, Chicago, IL 60611
Clarification on the decarboxylation mechanism in KasA based on the protonation state of key residues in the acyl-enzyme state.
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Institut für Physikalische und Theoretische Chemie, Universität Würzburg, Emil-Fischer Strasse 42, 97074, Würzburg, Germany.
The β-ketoacyl ACP synthase I (KasA) is a promising drug target because it is essential for the survival of Mycobacterium tuberculosis , a causative agent of tuberculosis. It catalyzes a condensation reaction that comprises three steps. The resulting elongated acyl chains are subsequently needed for the cell wall construction.
View Article and Find Full Text PDFCharacterization of chondroitin sulfate lyase ABC from Bacteroides thetaiotaomicron WAL2926.
Biochemistry
June 2008
Department of Biochemistry, McGill University, Montreal, Quebec, Canada.
Article Synopsis
- - Chondroitin sulfate ABC lyase (ChonABC) is an enzyme that breaks down chondroitin sulfate (CS) and dermatan sulfate (DS) glycosaminoglycans by cleaving glycosidic bonds, acting on different forms of uronic acid found in these compounds.
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Histidines 345 and 378 of Bacillus stearothermophilus leucine aminopeptidase II are essential for the catalytic activity of the enzyme.
Antonie Van Leeuwenhoek
May 2005
Department of Biology, Tung-Hai University, 181 Taichung-Kan Road, Taichung, Taiwan.
The conserved histidine residues, His-191, His-227, His-345, and His-378, in Bacillus stearothermophilus leucine aminopeptidase II (LAPII) were replaced with leucine by site-directed mutagenesis. The overexpressed wild-type and mutant enzymes have been purified by nickel-chelate chromatography and their molecular masses were approximately 44.5 kDa.
View Article and Find Full Text PDFThe catalytic cysteine and histidine in the plant acyl-acyl carrier protein thioesterases.
J Biol Chem
February 1996
Calgene, Inc., Davis, California 95616, USA.
The plant acyl-acyl carrier protein (acyl-ACP) thioesterases (TEs) play an essential role in chain termination during de novo fatty acid synthesis and are of biochemical interest because of their utilities in the genetic engineering of plant seed oils. Biochemical data have shown the possible involvement of an active-site cysteine and a histidine in catalysis, suggesting that these enzymes activate the hydrolysis of the thioester bond using the same basic catalytic machinery as those of proteases and lipases. To identify the cysteine and histidine residues that are critical in catalysis we substituted, in a 12:0 ACP TE (Uc FatB1), a conserved cysteine (Cys-320) to an Ala or a Ser, and three conserved histidines (His-140, His-285, and His-345) to an Ala or an Arg.
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