WebWe compared the eukaryotic serine racemase with bacterial alanine racemase, the best-studied enzyme among the PLP-dependent amino acid racemases, and thus suggested a putative reaction mechanism for mammalian D-serine synthesis. Publication types Research Support, Non-U.S. Gov't Review MeSH terms Alanine Racemase / chemistry* WebSep 12, 2013 · The 1.45 Å Crystal Structure of Alanine Racemase from a Pathogenic Bacterium, Pseudomonas aeruginosa. Contains both Internal and External Aldimine Structures Biochemistry, 2003, 42; 14752 2003
The structure of alanine racemase from Acinetobacter baumannii
WebFeb 8, 2005 · We report the crystal structure of alanine racemase from Mycobacterium tuberculosis (Alr(Mtb)) at 1.9 A resolution. In our structure, Alr(Mtb) is found to be a dimer formed by two crystallographically different monomers, each comprising 384 residues. The domain makeup of each monomer is similar to that of Bacillus and Pseudomonas alanine ... WebJul 20, 2024 · In the 'wild-type' (natural) alanine racemase reaction, an active site histidine (red in figure below) deprotonates a neighboring tyrosine residue (blue), which in turn acts as the catalytic base abstracting the α -proton of the substrate. simphiwe hamilton
The crystal structure of alanine racemase from
WebJul 1, 2014 · Alanine racemase (Alr) is a pyridoxal-5′-phosphate (PLP)-dependent enzyme that catalyzes the reversible racemization of l - and d-alanine. Since d -alanine is an … WebStructure of DCS-resistant variant D322N of alanine racemase from Mycobacterium tuberculosis WebSep 1, 2014 · The tertiary structure of A. baumannii alanine racemase (Alr Aba) is a homodimer in which the two monomers interact in a head-to-tail manner. This results in two active sites per enzyme, each comprised of residues from the N-terminal domain of one monomer and the C-terminal domain of the second monomer ... simphiwe hlophe home affairs