# The Pyridoxal-5′-Phosphate-Dependent Enzymes of Mycobacterium tuberculosis

## TL;DR

This paper explores the role of pyridoxal 5′-phosphate-dependent enzymes in Mycobacterium tuberculosis, focusing on their metabolic importance and potential as drug targets.

## Contribution

The study provides a comprehensive annotated catalog and analysis of PLP-dependent enzymes in M. tuberculosis, highlighting their roles and drug targeting potential.

## Key findings

- M. tuberculosis encodes 45 PLP-dependent enzymes, most of which are well-characterized.
- Some PLP-dependent enzymes are essential for survival and are targets of existing drugs like d-cycloserine.
- The study identifies enzymes with uncertain functions that could be key to understanding M. tuberculosis biology.

## Abstract

Enzymes that depend on the cofactor pyridoxal 5′-phosphate
(PLP) catalyze a remarkable variety of biochemical reactions in all
organisms. In particular, the genome of Mycobacterium
tuberculosis, the causative agent of tuberculosis
(TB), encodes 45 bona fide PLP-dependent enzymes plus a few related
proteins that presumably do not have enzymic function. The large majority
of the 45 enzymes have been characterized in terms of catalytic activity
and structure. Several of them have been shown to be central to the
bacterium’s survival and pathogenicity, while some of these
enzymes are targets of an extant drug (d-cycloserine). Herein,
the annotated catalog of the PLP-dependent enzymes in M. tuberculosis is presented and analyzed with three
main goals in mind. The first will be to assess the specific aspects
of mycobacterial metabolism that rely most on PLP-dependent enzymes.
A second goal will be to signal those enzymes whose function is still
uncertain and whose functional characterization may help to further
understand the biology of M. tuberculosis. Finally, we will examine the potential and limitations of targeting
the PLP-dependent enzymes for the development of new antimycobacterial
drugs.