<p>(A) L-Asparaginase tetramer with subunits highlighted with different colors, one active site is represented in red spheres, the pre-selected PEGylation positions in blue spheres, and the distances between mutated residues (A38C and T263C) are shown by black dotted lines. (B) L-Asparaginase dimer showing two active sites relatively buried (red spheres) in comparison with the PEGylations sites (blue spheres).</p
Background: Helicobacter pylori L-asparaginase is a recently isolated bacterial factor able to inhib...
In this paper, we have studied the catalytic mechanism of l-asparaginase II computationally. The rea...
Background: Helicobacter pylori L-asparaginase is a recently isolated bacterial factor able to inhib...
<p>(A) Mutant L-asparaginase (A38C-T263C) reduced with TCEP and eluted from the gel filtration colum...
<p>Relative catalytic activity is expressed as percentage compared to the non-conjugated L-asparagin...
(A) Electrophoresis (SDS-PAGE) showing the influence of PBS buffer ionic strength on N-terminal PEGy...
Enzymes capable of converting l-asparagine to l-aspartate can be classified as bacterial-type or pla...
L-Asparaginase is an enzyme successfully being used in the treatment of acute lymphoblastic leukemia...
Bacterial L-asparaginases are amidohydrolases (EC 3.5.1.1) capable of deaminating L-asparagine and, ...
Bacterial L-asparaginases are amidohydrolases (EC 3.5.1.1) capable of deaminating L-asparagine and, ...
Bacterial asparaginases (amidohydrolases, EC 3.5.1.1) are important enzymes in cancer therapy, espec...
Bacterial asparaginases (amidohydrolases, EC 3.5.1.1) are important enzymes in cancer therapy, espec...
<div><p>L-Asparaginase is an enzyme successfully being used in the treatment of acute lymphoblastic ...
L-asparaginase (ASNase) from Escherichia coli is currently used in some countries in its PEGylated f...
L-asparaginases (EC 3.5.1.1) are a family of enzymes that catalyze the hydrolysis of L-asparagine to...
Background: Helicobacter pylori L-asparaginase is a recently isolated bacterial factor able to inhib...
In this paper, we have studied the catalytic mechanism of l-asparaginase II computationally. The rea...
Background: Helicobacter pylori L-asparaginase is a recently isolated bacterial factor able to inhib...
<p>(A) Mutant L-asparaginase (A38C-T263C) reduced with TCEP and eluted from the gel filtration colum...
<p>Relative catalytic activity is expressed as percentage compared to the non-conjugated L-asparagin...
(A) Electrophoresis (SDS-PAGE) showing the influence of PBS buffer ionic strength on N-terminal PEGy...
Enzymes capable of converting l-asparagine to l-aspartate can be classified as bacterial-type or pla...
L-Asparaginase is an enzyme successfully being used in the treatment of acute lymphoblastic leukemia...
Bacterial L-asparaginases are amidohydrolases (EC 3.5.1.1) capable of deaminating L-asparagine and, ...
Bacterial L-asparaginases are amidohydrolases (EC 3.5.1.1) capable of deaminating L-asparagine and, ...
Bacterial asparaginases (amidohydrolases, EC 3.5.1.1) are important enzymes in cancer therapy, espec...
Bacterial asparaginases (amidohydrolases, EC 3.5.1.1) are important enzymes in cancer therapy, espec...
<div><p>L-Asparaginase is an enzyme successfully being used in the treatment of acute lymphoblastic ...
L-asparaginase (ASNase) from Escherichia coli is currently used in some countries in its PEGylated f...
L-asparaginases (EC 3.5.1.1) are a family of enzymes that catalyze the hydrolysis of L-asparagine to...
Background: Helicobacter pylori L-asparaginase is a recently isolated bacterial factor able to inhib...
In this paper, we have studied the catalytic mechanism of l-asparaginase II computationally. The rea...
Background: Helicobacter pylori L-asparaginase is a recently isolated bacterial factor able to inhib...