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B6db references: 29233695

type Journal Article
authors Son HF, Kim KJ
title Structural basis for substrate specificity of meso-diaminopimelic acid decarboxylase from Corynebacterium glutamicum
journal Biochem Biophys Res Commun
sel selected
ui 29233695
year (2018)
volume 495
number 2
pages 1815-1821
keywords Corynebacterium glutamicum; l-lysine biosynthesis; meso-diaminopimelic acid decarboxylase
abstract L-lysine is an essential amino acid that is widely used as a food supplement for humans and animals. meso-Diaminopimelic acid decarboxylase (DAPDC) catalyzes the final step in the de novol-lysine biosynthetic pathway by converting meso-diaminopimelic acid (meso-DAP) into l-lysine by decarboxylation reaction. To elucidate its molecular mechanisms, we determined the crystal structure of DAPDC from Corynebacterium glutamicum (CgDAPDC). The PLP cofactor is bound at the center of the barrel domain and forms a Schiff base with the catalytic Lys75 residue. We also determined the CgDAPDC structure in complex with both pyridoxal 5'-phosphate (PLP) and the l-lysine product and revealed that the protein has an optimal substrate binding pocket to accommodate meso-DAP as a substrate. Structural comparison of CgDAPDC with other amino acid decarboxylases with different substrate specificities revealed that the position of the α15 helix in CgDAPDC and the residues located on the helix are crucial for determining the substrate specificities of the amino acid decarboxylases.
last changed 2018/04/03 14:41

B6db references