<p>(A) Wild-type bglTm. (B) Mutant T1. (C) Mutant T2. The tested substrates were <i>p</i>-nitrophenyl β-glucopyranoside (NPβGlc) and <i>p</i>-nitrophenyl β-fucopyranoside (NPβFuc). Lines indicate the best fits of the experimental data (dots) using the appropriate kinetic equation (see the <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0191282#sec002" target="_blank">Materials and Methods</a> for details).</p
<p>(A) Structure of BglB in complex with the modeled <i>p</i>-nitrophenyl-β-D-glucoside (pNPG) used ...
<p>Hydrolysis was carried out at 37°C at in 20 mM MES buffer, pH 6.5. Substrate concentrations were ...
<p>A–B) [<i>P</i>] as a function of time for enzyme catalyzed hydrolysis of alanine-4-nitroanilide b...
<p>Kinetic parameters for the substrate hydrolysis by the wild-type and mutant Sfβgly.</p
<p>(A) MFA (B) MCA (C) MSA (D) M<i>p</i>CA. Black circle: wild type; white circle: P5; black triangl...
<p><b>A)</b> Wild type enzyme (gray bars) exhibited preference for nucleoside diphosphate sugar (NDP...
<p>Hydrolysis rates for substrates <i>p</i>NPG (A) and <i>t</i>ZOG (B) by β-glucosidase Zm-p60.1 var...
<p>Apparent kinetic parameters for hydrolysis of chloropropionate substrates by wild type and mutant...
<p>Each mutant gets a bar with six colored boxes, depicting 1) soluble protein expression, 2) T<sub>...
a<p>pNP, <i>p</i>-nitrophenyl.</p>b<p>A linear relationship between initial velocity (<i>v</i>) and ...
<p>The graph shows reaction velocities of JEV NS2B(H)-NS3(pro) for hydrolysis of Boc-GRR-amc (A); Bo...
<p>Red, wild-type bglTm; blue, T1 mutant; green, T2 mutant. The stability of the wild-type bglTm pro...
<p>Hydrolytic activities at 1.25 mM of pNPG were determined in the presence of glucose. ■, WT; ●, th...
<p>The rate of substrate Suc-LLVY-AMC hydrolysis (a release of AMC molecule) with control and inhibi...
Changes in substrate concentration were shown to affect the experimental maximum degree of hydrolysi...
<p>(A) Structure of BglB in complex with the modeled <i>p</i>-nitrophenyl-β-D-glucoside (pNPG) used ...
<p>Hydrolysis was carried out at 37°C at in 20 mM MES buffer, pH 6.5. Substrate concentrations were ...
<p>A–B) [<i>P</i>] as a function of time for enzyme catalyzed hydrolysis of alanine-4-nitroanilide b...
<p>Kinetic parameters for the substrate hydrolysis by the wild-type and mutant Sfβgly.</p
<p>(A) MFA (B) MCA (C) MSA (D) M<i>p</i>CA. Black circle: wild type; white circle: P5; black triangl...
<p><b>A)</b> Wild type enzyme (gray bars) exhibited preference for nucleoside diphosphate sugar (NDP...
<p>Hydrolysis rates for substrates <i>p</i>NPG (A) and <i>t</i>ZOG (B) by β-glucosidase Zm-p60.1 var...
<p>Apparent kinetic parameters for hydrolysis of chloropropionate substrates by wild type and mutant...
<p>Each mutant gets a bar with six colored boxes, depicting 1) soluble protein expression, 2) T<sub>...
a<p>pNP, <i>p</i>-nitrophenyl.</p>b<p>A linear relationship between initial velocity (<i>v</i>) and ...
<p>The graph shows reaction velocities of JEV NS2B(H)-NS3(pro) for hydrolysis of Boc-GRR-amc (A); Bo...
<p>Red, wild-type bglTm; blue, T1 mutant; green, T2 mutant. The stability of the wild-type bglTm pro...
<p>Hydrolytic activities at 1.25 mM of pNPG were determined in the presence of glucose. ■, WT; ●, th...
<p>The rate of substrate Suc-LLVY-AMC hydrolysis (a release of AMC molecule) with control and inhibi...
Changes in substrate concentration were shown to affect the experimental maximum degree of hydrolysi...
<p>(A) Structure of BglB in complex with the modeled <i>p</i>-nitrophenyl-β-D-glucoside (pNPG) used ...
<p>Hydrolysis was carried out at 37°C at in 20 mM MES buffer, pH 6.5. Substrate concentrations were ...
<p>A–B) [<i>P</i>] as a function of time for enzyme catalyzed hydrolysis of alanine-4-nitroanilide b...