A general correction to catalytic rates determined for nonprocessive exo-depolymerases acting on both substrate and product in the initial-rate measurement.
- Resource Type
- Academic Journal
- Authors
- Stoller JR; USDA-ARS-National Center for Agricultural Utilization Research, Peoria, IL 61604, USA.; Wagschal K; USDA-ARS-Western Regional Research Center, 800 Buchanan Street, Albany, CA 94710, USA.; Lee CC; USDA-ARS-Western Regional Research Center, 800 Buchanan Street, Albany, CA 94710, USA.; Jordan DB; USDA-ARS-National Center for Agricultural Utilization Research, Peoria, IL 61604, USA. Electronic address: douglas.jordan@ars.usda.gov.
- Source
- Publisher: Elsevier Country of Publication: United States NLM ID: 0370535 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1096-0309 (Electronic) Linking ISSN: 00032697 NLM ISO Abbreviation: Anal Biochem Subsets: MEDLINE
- Subject
- Language
- English
We recently reported on the kinetics of the polygalacturonase TtGH28 acting on trimer and dimer substrates. When the starting substrate for hydrolysis is the trimer, the product dimer is also subject to hydrolysis, resulting in discrepancies when either the concentration of dimer or monomer product is used for analysis of trimer hydrolysis. Here, we derive a method for determining catalytic rates of exo-hydrolases acting on trimer (and higher order) substrates when products may also be substrates for hydrolysis and show how this correction may be applied for TtGH28.
(Published by Elsevier Inc.)