Pyridoxal 5′-phosphate enzymes are ubiquitous in the nitrogen metabolism of all
organisms. They catalyze a wide variety of reactions including racemization, transamination …

In plants, cysteine biosynthesis plays a central role in fixing inorganic sulfur from the
environment and provides the only metabolic sulfide donor for the generation of methionine …

Cysteine is the final product of the reductive sulfate assimilation pathway in bacteria and
plants and serves as the precursor for all sulfur-containing biological compounds, such as …

Cysteine biosynthetic genes are up-regulated in the persistent phase of Mycobacterium
tuberculosis, and the corresponding enzymes are therefore of interest as potential targets for …

Pyridoxal 5′-phosphate (PLP; vitamin B6)-catalyzed reactions have been well studied, both
on enzymes and in solution, due to the variety of important reactions this cofactor catalyzes …

The biosynthesis of cysteine is a crucial metabolic pathway supplying a building block for de
novo protein synthesis but also a reduced thiol as a component of the oxidative defense …

Trichomonas vaginalis is an early divergent eukaryote with many unusual biochemical
features. It is an anaerobic protozoan parasite of humans that is thought to rely heavily on …

Mycobacterium tuberculosis is dependent on cysteine biosynthesis, and reduced sulfur
compounds such as mycothiol synthesized from cysteine serve in first-line defense …

The kinetic pathway of CysM, a cysteine synthase from Mycobacterium tuberculosis, was
studied by transient-state kinetic techniques. The expression of which is upregulated under …

O-Acetylserine sulfhydrylase is a pyridoxal 5′-phosphate (PLP)-dependent enzyme that
catalyzes the final step in the cysteine biosynthetic pathway in enteric bacteria and plants …