Bifunctional Substrate Activation via an Arginine Residue Drives Catalysis in Chalcone Isomerases
نویسندگان
چکیده
منابع مشابه
Bifunctional catalysis
Bifunctional catalysis concerns the use of low molecular weight, structurally defined molecules possessing two distinct functional groups to bring about new reactivity and/or selectivity in a reaction of interest. The reactions are typically polar addition reactions of pronucleophiles and electrophiles where, ideally, simple low-cost starting materials are converted into high-value, stereochemi...
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Reaction of phenylglyoxal, a reagent specific for arginine residues, with porcine phospholipase Az results in complete elimination of catalytic activity. The modification reaction is markedly dependent on pH. Other dicarbonyl compounds such as 2,3-butanedione and 1,2cyclohexanedione also react with the enzyme to cause loss of activity but at significantly slower rates. At pH 7.0, the inactivati...
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All sphingolipid-producing organisms require the pyridoxal 5'-phosphate (PLP)-dependent serine palmitoyltransferase (SPT) to catalyse the first reaction on the de novo sphingolipid biosynthetic pathway. SPT is a member of the alpha oxoamine synthase (AOS) family that catalyses a Claisen-like condensation of palmitoyl-CoA and L-serine to form 3-ketodihydrosphingosine (KDS). Protein sequence alig...
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Acetolatate synthase(ALS) catalyzes the first common step in the biosynthesis of valine, leucine, isoleucine in plants and microorganisms. ALS is the target of several classes of herbicides, including the sulfonylureas, the imidazolinones, and the triazolopyrimidines. To elucidate the roles of arginine residues in tobacco ALS, chemical modification and site-directed mutagenesis were performed. ...
متن کاملArginine deiminase uses an active-site cysteine in nucleophilic catalysis of L-arginine hydrolysis.
Arginine deiminase (EC 3.5.3.6) catalyzes the hydrolysis of l-arginine to citrulline and ammonium ion, which is the first step of the microbial l-arginine degradation pathway. The deiminase conserves the active-site Cys-His-Asp motif found in several related enzymes that catalyze group-transfer reactions from the guanidinium center of arginine-containing substrates. For each of these enzymes, n...
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ژورنال
عنوان ژورنال: ACS Catalysis
سال: 2019
ISSN: 2155-5435,2155-5435
DOI: 10.1021/acscatal.9b01926