Background: D-Phenylglycine aminotransferase (D-PhgAT) is highly beneficial in pharmaceutical biotechnology. Like many other enzymes, D-PhgAT suffers from low stability under harsh processing conditions, poor solubility of substrate, products and occasional microbial contamination. Incorporation of miscible organic solvents into the enzyme’s reaction is considered as a solution...

D-Phenylglycine aminotransferase (D-PhgAT) from Pseudomonas stutzeri ST-201 is useful for enzymatic synthesis of enantiomerically pure D-phenylglycine. However, its low protein solubility prevents its application at high substrate concentration. With an aim to increase the protein solubility, the N-terminus of D-PhgAT was genetically fused with short peptides (A1 α- helix, A2 α-helix, and ALAL,...

BACKGROUND D-phenylglycine aminotransferase (D-PhgAT) of Pseudomonas stutzeri ST-201 catalyzes the reversible stereo-inverting transamination potentially useful in the application for synthesis of D-phenylglycine and D-4-hydroxyphenylglycine using L-glutamate as a low cost amino donor substrate in one single step. The enzyme is a relatively hydrophobic homodimeric intracellular protein difficul...

The aim of this study was to enhance the bond strength of one-step bonding agents to dentin. In particular, the focus was on using Catabrush the applicator system of AQ Bond Plus. Catabrush was supplemented with N-phenylglycine and aromatic sulfinate as polymerization accelerators, as N-phenylglycine was reportedly beneficial in improving the bond strength to dentin. The results indicated that ...

Molecular interaction between nucleic acid bases and amino acids is a fundamental process in biology. The adsorption of the molecules on surfaces provides the opportunity to study such interactions in great detail by exploiting the high-resolution imaging capabilities of scanning tunnelling microscopy (STM). The chemisorption of prochiral molecules, such as adenine, on a metal surface causes th...

Cephalexin synthesizing enzyme (CSE) of Gluconobacter oxydans ATCC 9324 was purified up to about 940-fold at a yield of 12%. CSE biosynthesis in G. oxydans was found inducible in the presence of D-phenylglycine but not its substrate phenylglycine methyl ester. The purified enzyme was shown homogeneous on SDS-PAGE and exhibited a specific activity of 440 U per mg protein. The apparent molecular ...

The conversion of rac -phenylglycinonitrile by different variants the nitrilase from Pseudomonas fluorescens EBC191 (EC 3.5.5.1) was studied and amounts chiral composition formed phenylglycine amide compared. Muteins that converted to extraordinarily high or were tested for chemoenzymatic enantioselective one-pot synthesis ( R )- S )-phenylglycine amide. combined initial step in traditional che...