Structure of ALD1, a Plant-specific Homologue of the Universal Diaminopimelate Aminotransferase Enzyme of Lysine Biosynthesis

Overview

Journal Acta Crystallogr Sect F Struct Biol Cryst Commun

Date 2013 Feb 7

PMID 23385743

Citations 5

Authors

Vladimir Sobolev

Marvin Edelman

Orly Dym

Tamar Unger

Shira Albeck

Menny Kirma

Gad Galili

Affiliations

Soon will be listed here.

Abstract

Diaminopimelate aminotransferase (DAP-AT) is an enzyme in the lysine-biosynthesis pathway. Conversely, ALD1, a close homologue of DAP-AT in plants, uses lysine as a substrate in vitro. Both proteins require pyridoxal-5'-phosphate (PLP) for their activity. The structure of ALD1 from the flowering plant Arabidopsis thaliana (AtALD1) was solved at a resolution of 2.3 Å. Comparison of AtALD1 with the previously solved structure of A. thaliana DAP-AT (AtDAP-AT) revealed similar interactions with PLP despite sequence differences within the PLP-binding site. However, sequence differences between the binding site of AtDAP-AT for malate, a purported mimic of substrate binding, and the corresponding site in AtALD1 led to different interactions. This suggests that either the substrate itself, or the substrate-binding mode, differs in the two proteins, supporting the known in vitro findings.

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