Structural biology of proline catabolism.

John J Tanner
Author Information
  1. John J Tanner: Departments of Chemistry and Biochemistry, University of Missouri, Columbia, MO 65211, USA. tannerjj@missouri.edu

Abstract

The proline catabolic enzymes proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase catalyze the 4-electron oxidation of proline to glutamate. These enzymes play important roles in cellular redox control, superoxide generation, apoptosis and cancer. In some bacteria, the two enzymes are fused into the bifunctional enzyme, proline utilization A. Here we review the three-dimensional structural information that is currently available for proline catabolic enzymes. Crystal structures have been determined for bacterial monofunctional proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase, as well as the proline dehydrogenase and DNA-binding domains of proline utilization A. Some of the functional insights provided by analyses of these structures are discussed, including substrate recognition, catalytic mechanism, biochemical basis of inherited proline catabolic disorders and DNA recognition by proline utilization A.

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Grants

  1. R01 GM065546/NIGMS NIH HHS
  2. R01 GM065546-04/NIGMS NIH HHS
  3. GM065546/NIGMS NIH HHS

MeSH Term

Bacterial Proteins
Crystallography, X-Ray
Databases, Protein
Humans
Membrane Proteins
Models, Biological
Models, Chemical
Molecular Conformation
Oxidation-Reduction
Phylogeny
Proline
Proline Oxidase
Protein Conformation
Protein Folding
Protein Structure, Secondary
Protein Structure, Tertiary

Chemicals

Bacterial Proteins
Membrane Proteins
PutA protein, Bacteria
Proline
Proline Oxidase

Word Cloud

Created with Highcharts 10.0.0prolinedehydrogenaseenzymescatabolicutilizationDelta1-pyrroline-5-carboxylatestructuresrecognitioncatalyze4-electronoxidationglutamateplayimportantrolescellularredoxcontrolsuperoxidegenerationapoptosiscancerbacteriatwofusedbifunctionalenzymereviewthree-dimensionalstructuralinformationcurrentlyavailableCrystaldeterminedbacterialmonofunctionalwellDNA-bindingdomainsfunctionalinsightsprovidedanalysesdiscussedincludingsubstratecatalyticmechanismbiochemicalbasisinheriteddisordersDNAAStructuralbiologycatabolism

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