Structural biology of proline catabolism
1Departments of Chemistry and Biochemistry, University of Missouri, Columbia, MO 65211, USA. tannerjj@missouri.edu
Amino Acids
|March 29, 2008
Summary
Structural insights into proline catabolic enzymes reveal their roles in cellular processes and disease. This review covers crystal structures of key enzymes involved in proline oxidation and DNA binding.
Area of Science:
- Biochemistry
- Structural Biology
- Enzymology
Background:
- Proline catabolic enzymes, proline dehydrogenase (PDH) and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), are crucial for cellular redox control, superoxide generation, apoptosis, and cancer.
- These enzymes catalyze the oxidation of proline to glutamate.
- In bacteria, a bifunctional enzyme, proline utilization A (PutA), contains both PDH and P5CDH activities, along with a DNA-binding domain.
Purpose of the Study:
- To review available three-dimensional structural information for proline catabolic enzymes.
- To discuss functional insights derived from these structures, including substrate recognition and catalytic mechanisms.
- To explore the structural basis of inherited proline catabolic disorders and DNA recognition by PutA.
Main Methods:
- X-ray crystallography was used to determine the structures of bacterial monofunctional PDH and P5CDH.
- Crystal structures of the PDH and DNA-binding domains of the bifunctional PutA were also determined.
Main Results:
- Detailed structural information is available for bacterial monofunctional proline catabolic enzymes.
- Structural data for key domains of the bifunctional proline utilization A enzyme, including its DNA-binding region, have been elucidated.
- Analysis of these structures provides insights into enzyme function and substrate interactions.
Conclusions:
- Structural studies of proline catabolic enzymes offer critical insights into their biological roles and mechanisms.
- Understanding these structures can illuminate the biochemical basis of inherited metabolic disorders related to proline catabolism.
- The structural information is vital for understanding the dual enzymatic and DNA-binding functions of PutA.
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