First Evidence for Substrate Channeling between Proline Catabolic Enzymes A VALIDATION OF DOMAIN FUSION ANALYSIS FOR PREDICTING PROTEIN-PROTEIN INTERACTIONS

Authors

• Nikhilesh Sanyal, University of Nebraska-LincolnFollow
• Benjamin W. Arentson, University of Nebraska-LincolnFollow
• John J. Tanner, University of Missouri-Columbia, Columbia, MOFollow
• Donald F. Becker, University of Nebraska-LincolnFollow

Document Type

Article

Date of this Version

2015

Citation

THE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 290, NO. 4, pp. 2225–2234, January 23, 2015

Comments

© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.

Abstract

Background: PRODH and P5CDH from Thermus thermophilus are monofunctional enzymes in proline catabolism.

Results: Steady-state kinetics and intermediate trapping data show the PRODH and P5CDH reactions are coupled by a channeling step.

Conclusion: Substrate channeling in monofunctional enzymes is achieved via weak interactions.

Significance: Evidence for substrate channeling between monofunctional proline catabolic enzymes is shown and confirms the Rosetta Stone hypothesis.