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Amino Acids. 2008 Nov;35(4):719-30. doi: 10.1007/s00726-008-0062-5. Epub 2008 Mar 28.

Structural biology of proline catabolism.

Author information

1
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.

PMID:
18369526
PMCID:
PMC2664619
DOI:
10.1007/s00726-008-0062-5
[Indexed for MEDLINE]
Free PMC Article

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