Crystal structure of maize serine racemase with pyridoxal 5 ′ -phosphate

Serine racemase (SR) is a pyridoxal 5 ′ -phosphate (PLP)-dependent enzyme that is responsible for d-serine biosynthesis in vivo. The first X-ray crystal structure of maize SR was determined to 2.1   Å resolution and PLP binding was confirmed in solution by UV – Vis absorption spectrometry. Maize SR belongs to the type II PLP-dependent enzymes and differs from the SR of a vancomycin-resistant bacterium. The PLP is bound to each monomer by forming a Schiff base with Lys67. Structural comparison with rat and fission yeast SRs reveals a similar arrangement of active-site residues but a different orientation of the C-terminal helix.

Source: Acta Crystallographica Section F - February 15, 2016 Category: Biochemistry Authors: Zou, L. Song, Y. Wang, C. Sun, J. Wang, L. Cheng, B. Fan, J. Tags: structural comparison serine racemase maize crystal structure cofactor pyridoxal 5 ′ -phosphate research communications Source Type: research