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  • enzyme
  • All substrates were dephosphorylated by AtZDP, assuming that this enzyme could potentially be involved in double-strand DNA repair. (diva-portal.org)
  • in this way it has been shown that the prodigiosin synthesising enzyme, PigC, has a relaxed substrate-specificity. (rsc.org)
  • Enzyme activity and substrate specificity of the major cinnamyl alcohol dehydrogenases in sorghum. (plantphysiol.org)
  • The result is a polymerase that is kinetically indistinguishable from the wild-type enzyme, but provides a signal to monitor changes in enzyme structure that result from conformational changes induced by substrate binding. (utexas.edu)
  • These results were rationalized based on the enzyme-substrate interactions observed in a homology model with a docked ligand. (ugent.be)
  • This assay provides a quick and efficient method to screen the substrate specificity of para -phenol oxidases, facilitating the enzyme engineering of known para- phenol oxidases and the evaluation of the substrate specificity of novel para -phenol oxidases. (mdpi.com)
  • It catalyses the condensation of tryptamine with secologanin to form strictosidine: tryptamine + secologanin ⇌ {\displaystyle \rightleftharpoons } 3-alpha(S)-strictosidine + H2O Thus, the two substrates of this enzyme are tryptamine and secologanin, whereas its two products are 3-alpha(S)-strictosidine and H2O. (wikipedia.org)
  • In enzymology, a tryptophan alpha,beta-oxidase (EC 1.3.3.10) is an enzyme that catalyzes the chemical reaction L-tryptophan + O2 ⇌ {\displaystyle \rightleftharpoons } alpha,beta-didehydrotryptophan + H2O2 Thus, the two substrates of this enzyme are L-tryptophan and O2, whereas its two products are alpha,beta-didehydrotryptophan and H2O2. (wikipedia.org)
  • In enzymology, a haloalkane dehalogenase (EC 3.8.1.5) is an enzyme that catalyzes the chemical reaction 1-haloalkane + H2O ⇌ {\displaystyle \rightleftharpoons } a primary alcohol + halide Thus, the two substrates of this enzyme are 1-haloalkane and H2O, whereas its two products are primary alcohol and halide. (wikipedia.org)
  • In enzymology, a trypanothione-disulfide reductase (EC 1.8.1.12) is an enzyme that catalyzes the chemical reaction trypanothione + NADP+ ⇌ {\displaystyle \rightleftharpoons } trypanothione disulfide + NADPH + H+ Thus, the two substrates of this enzyme are trypanothione and NADP+, whereas its 3 products are trypanothione disulfide, NADPH, and H+. (wikipedia.org)
  • In enzymology, a riboflavin kinase (EC 2.7.1.26) is an enzyme that catalyzes the chemical reaction ATP + riboflavin ⇌ {\displaystyle \rightleftharpoons } ADP + FMN Thus, the two substrates of this enzyme are ATP and riboflavin, whereas its two products are ADP and FMN. (wikipedia.org)
  • In enzymology, an estradiol 17beta-dehydrogenase (EC 1.1.1.62) is an enzyme that catalyzes the chemical reaction estradiol-17beta + NAD(P)+ ⇌ {\displaystyle \rightleftharpoons } estrone + NAD(P)H + H+ The 3 substrates of this enzyme are estradiol-17beta, NAD+, and NADP+, whereas its 4 products are estrone, NADH, NADPH, and H+. (wikipedia.org)
  • They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor: RCH2NH2 + H2O + O2 ⇌ {\displaystyle \rightleftharpoons } RCHO + NH3 + H2O2 The 3 substrates of this enzyme are primary amines (RCH2NH2), H2O, and O2, whereas its 3 products are RCHO, NH3, and H2O2. (wikipedia.org)
  • In prokaryotes, the enzyme enables various amine substrates to be used as sources of carbon and nitrogen. (wikipedia.org)
  • kinetics
  • Additionally, we have characterized the kinetics governing the specificity and discrimination of several widely administered Nucleotide Reverse Transcriptase Inhibitors (NRTI's) used to combat HIV infection including 3TC (Lamivudine), FTC (Emtricitabine), and AZT (Zidovudine) for the wild-type polymerase and mutants with clinical resistance to these compounds. (utexas.edu)
  • cleavage
  • The essential role of hemopexin carboxyl-domain exosites in the cleavage of noncollagenous substrates such as chemokines has also been recently revealed. (springer.com)
  • This article updates a previous review of the role of substrate recognition by MMP exosites in both preparing complex substrates, such as collagen, for cleavage and for tethering noncollagenous substrates to MMPs for more efficient proteolysis. (springer.com)
  • The potential role of collagen binding in regulating MMP-2 (gelatinase A) activation at the cell surface reveals unexpected consequences of substrate interactions that can lead to collagen cleavage and regulation of the activation and activity of downstream proteinases necessary to complete the collagenolytic cascade. (springer.com)
  • Other endoglycosidases, similar to PNGase F, include endoglycosidase F1, endoglycosidase F2, endoglycosidase F3, and endoglycosidase H. These endoglycosidases have more specificity in cleavage and are less sensitive to protein conformation than PNGase F. All of these endoglycosidases, including PNGase F, can be purified from an almond emulsion or flavobacterium meningosepticum. (wikipedia.org)
  • alterations
  • Screening of a small library of VAO and EUGO active-site variants for alterations in their substrate specificity led to the identification of a VAO variant (T457Q) with increased activity towards vanillyl alcohol (4-hydroxy-3-methoxybenzyl alcohol) and a EUGO variant (V436I) with increased activity towards chavicol (4-allylphenol) and 4-cyclopentylphenol. (mdpi.com)
  • 1991
  • 1991) "Protein Kinase C Substrate and Inhibitor Characteristics of Peptides Derived From the Myristoylated Alanine-Rich C Kinase Substrate (MARCKS) Protein Phosphorylation Site Domain" The Journal of Biological Chemistry266(22):14390-14398. (patentgenius.com)
  • kinetic
  • The substrate specificity was investigated in detail by measuring the relative activity on a range of alternative acceptors, applied in the reverse synthetic reaction, and determination of the kinetic parameters for the best acceptors. (ugent.be)
  • affinity
  • Interestingly, the abrogation of the LeuRS specificity determinant threonine 252 did not improve the affinity of the editing site for the cognate leucine as expected, but instead substantially enhanced the rate of leucyl-tRNA Leu hydrolysis. (elsevier.com)
  • domain
  • The importance of discrete MMP substrate binding sites termed exosites on domains located outside the catalytic domain was first demonstrated for native collagenolysis. (springer.com)
  • The origin of specificity of the LeuRS editing domain was until now unresolved. (elsevier.com)
  • Interestingly, loops from the first SH3b domain dock into the ends of the active site groove of the catalytic domain, remodel the substrate binding site, and modulate substrate specificity. (osti.gov)
  • activity
  • Substrate preferences at P5 to P3 positions were important in enhancing the main protease activity. (hkmj.org)
  • Super-reactive' substrate sequences were engineered, with more than a 2-fold increase in activity, by combining the best residue choices at P5 to P3 positions. (hkmj.org)
  • The assay was used to screen the activity of VAO and EUGO towards a set of twenty-four potential substrates. (mdpi.com)
  • effects
  • Since both phosphorylation and O-GlcNAcylation compete for similar serine or threonine residues, the two processes may compete for sites, or they may alter the substrate specificity of nearby sites by steric or electrostatic effects. (wikipedia.org)
  • role
  • We further established the critical role for the A76 3′-OH group of the tRNA Leu in post-transfer editing, which supports the substrate-assisted deacylation mechanism. (elsevier.com)
  • In doing so, we define the role of induced-fit in nucleotide specificity and mismatch discrimination. (utexas.edu)
  • variety
  • The Walker A motif is best known for its presence in ATP- and GTP-binding proteins, and is also found in a variety of proteins with phosphorylated substrates. (wikipedia.org)
  • mechanism
  • Activation of the dispensing mechanism of the cleaning device may dispense a metered dose of composition, in a generally horizontal direction, onto and/or into a nonwoven or other substrate. (patents.com)
  • Although the exact binding mechanism to the nitrile substrate still remains unknown, by drawing comparisons between the sequence and structure with other nitrilases, the catalytic triad was determined to consist of Glu 42, Lys 113, and Cys 146. (wikipedia.org)
  • displaystyle
  • In enzymology, a mannitol dehydrogenase (EC 1.1.1.255) is an enzyme that catalyzes the chemical reaction D-mannitol + NAD+ ⇌ {\displaystyle \rightleftharpoons } D-mannose + NADH + H+ Thus, the two substrates of this enzyme are D-mannitol and NAD+, whereas its 3 products are D-mannose, NADH, and H+. (wikipedia.org)
  • In enzymology, a glycerophosphoinositol inositolphosphodiesterase (EC 3.1.4.43) is an enzyme that catalyzes the chemical reaction 1-(sn-glycero-3-phospho)-1D-myo-inositol + H2O ⇌ {\displaystyle \rightleftharpoons } glycerol + 1D-myo-inositol 1-phosphate Thus, the two substrates of this enzyme are 1-(sn-glycero-3-phospho)-1D-myo-inositol and H2O, whereas its two products are glycerol and 1D-myo-inositol 1-phosphate. (wikipedia.org)
  • In enzymology, a demethylmacrocin O-methyltransferase (EC 2.1.1.102) is an enzyme that catalyzes the chemical reaction S-adenosyl-L-methionine + demethylmacrocin ⇌ {\displaystyle \rightleftharpoons } S-adenosyl-L-homocysteine + macrocin Thus, the two substrates of this enzyme are S-adenosyl methionine and demethylmacrocin, whereas its two products are S-adenosylhomocysteine and macrocin. (wikipedia.org)
  • p a l m i t o y l − S C o A + H 2 O ⇄ C o A S H + p a l m i t a t e {\displaystyle palmitoyl-SCoA+H_{2}O\rightleftarrows CoASH+palmitate} Thus, the two substrates of this enzyme are palmitoyl-CoA and H2O, whereas its two products are CoA and palmitate. (wikipedia.org)
  • In enzymology, a cholesterol 24-hydroxylase (EC 1.14.13.98) is an enzyme that catalyzes the chemical reaction cholesterol + NADPH + H+ + O2 ⇌ {\displaystyle \rightleftharpoons } (24S)-24-hydroxycholesterol + NADP+ + H2O The 4 substrates of this enzyme are cholesterol, NADPH, H+, and O2, whereas its 3 products are (24S)-24-hydroxycholesterol, NADP+, and H2O. (wikipedia.org)
  • chains
  • Based on their action specificity toward α-glucan chains they are either exo-acting (α-amylase and glucoamylase) or endo-acting in nature. (frontiersin.org)
  • Cholesterol-24 hydroxylase has a variety of possible substrates, including: elongated steroid chains, cholesterol derivatives, and a variety of drug candidates. (wikipedia.org)
  • high
  • First, antibodies with high specificities for plant SPS also target the bacterial SPS, indicating the structure is conserved enough for the antibody to recognize the enzyme as an antigen. (wikipedia.org)
  • domain
  • In this closed conformation, the Gly-34 residue of the A domain interacts with UDP-glucose and forces the substrate to adapt a folded structure, facilitating its donation of the hexosyl group. (wikipedia.org)
  • addition
  • Early release of the enzyme-bound substrate after the first water hydrolysis followed by delayed addition of the second water Low temperature and increased pH conditions. (wikipedia.org)