2014
DOI: 10.1074/jbc.m113.523704
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Evidence for Hysteretic Substrate Channeling in the Proline Dehydrogenase and Δ1-Pyrroline-5-carboxylate Dehydrogenase Coupled Reaction of Proline Utilization A (PutA)

Abstract: Background:PutA from Escherichia coli is a bifunctional enzyme and transcriptional repressor in proline catabolism. Results: Steady-state and transient kinetic data revealed a mechanism in which the two enzymatic reactions are coupled by an activation step. Conclusion: Substrate channeling in PutA exhibits hysteretic behavior. Significance: This is the first kinetic model of bi-enzyme activity in PutA and reveals a novel mechanism of channeling activation.

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Cited by 30 publications
(72 citation statements)
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References 52 publications
(81 reference statements)
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“…The observed lag time is greater than that observed for PutA. The lag times reported for PutA enzymes thus far range from no apparent lag to 23 s for E. coli PutA (8,9,11). The longer lag time of the TtPRODH- (50).…”
Section: Discussionmentioning
confidence: 66%
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“…The observed lag time is greater than that observed for PutA. The lag times reported for PutA enzymes thus far range from no apparent lag to 23 s for E. coli PutA (8,9,11). The longer lag time of the TtPRODH- (50).…”
Section: Discussionmentioning
confidence: 66%
“…Blockage of the tunnel in B. japonicum PutA by mutagenesis abrogates channeling, which indicates that the tunnel functions as the conduit for the intermediate P5C/GSA (10). Furthermore, a substrate channeling mechanism is supported by kinetic studies of PutA from Escherichia coli (11) and Salmonella typhimurium (12) indicating that a general feature of PutA enzymes is direct transfer of P5C between the PRODH and P5CDH active sites.…”
mentioning
confidence: 63%
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