Adaptation of a synthesis method for acetyl phosphate to related substrates
- 1Department of Biological Sciences, University of Wisconsin-Parkside, Kenosha, WI 53141-2000, USA
- 2Department of Chemistry, University of Wisconsin-Parkside, Kenosha, WI 53141-2000, USA
Abstract
Acyl phosphate substrate availability is critical for applicable biochemical studies. Accordingly, various synthesis methods have been developed over the years typically focused on acetyl phosphate. One of these synthesis methods was proven versatile, capable of producing assorted primary and secondary acyl phosphates with high purity as measured by NMR spectroscopy, total carbon analysis and hydroxamate assays. Biochemical activity assays using synthesized acyl phosphate substrates generate results consistent with previously published kinetic constant data for Methanosarcina thermophila acetate kinase, while kinetic constant results for new substrates are reported for both M. thermophila acetate kinase and Desulfovibrio vulgaris str. Hildenborough butyrate kinase.
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BibTeX
@article{rodriguez2026adaptation,
title = {{Adaptation of a synthesis method for acetyl phosphate to related substrates}},
author = {Adrianna M. Rodriguez and Stefinie Washington and Radhika Ramesh and Malinda M. Batassa and Snigdha Reddy and Lori B. Allen and Ilirian Dhimitruka and Robert D. Barber},
journal = {Analytical biochemistry},
year = {2026},
month = sep,
doi = {10.1016/j.ab.2026.116261},
url = {https://doi.org/10.1016/j.ab.2026.116261},
note = {CC BY},
}
RIS
TY - JOUR
TI - Adaptation of a synthesis method for acetyl phosphate to related substrates
AU - Adrianna M. Rodriguez
AU - Stefinie Washington
AU - Radhika Ramesh
AU - Malinda M. Batassa
AU - Snigdha Reddy
AU - Lori B. Allen
AU - Ilirian Dhimitruka
AU - Robert D. Barber
PY - 2026
DA - 2026/09/30
JO - Analytical biochemistry
DO - 10.1016/j.ab.2026.116261
UR - https://doi.org/10.1016/j.ab.2026.116261
AB - Acyl phosphate substrate availability is critical for applicable biochemical studies. Accordingly, various synthesis methods have been developed over the years typically focused on acetyl phosphate. One of these synthesis methods was proven versatile, capable of producing assorted primary and secondary acyl phosphates with high purity as measured by NMR spectroscopy, total carbon analysis and hydroxamate assays. Biochemical activity assays using synthesized acyl phosphate substrates generate results consistent with previously published kinetic constant data for Methanosarcina thermophila acetate kinase, while kinetic constant results for new substrates are reported for both M. thermophila acetate kinase and Desulfovibrio vulgaris str. Hildenborough butyrate kinase.
SN - 0003-2697
SN - 1096-0309
ER -