Non-Steady State Analysis of Enzyme Kinetics in Real Time Elucidates Substrate Association and Dissociation Rates: Demonstration with Analysis of Firefly Luciferase Mutants-Reference-Cited by-同舟云学术

Non-Steady State Analysis of Enzyme Kinetics in Real Time Elucidates Substrate Association and Dissociation Rates: Demonstration with Analysis of Firefly Luciferase Mutants

Published:2019-05-22 Issue:23 Volume:58 Page:2695-2702
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Dale Renee¹²,Ohmuro-Matsuyama Yuki³,Ueda Hiroshi³^ORCID,Kato Naohiro¹^ORCID

Affiliation:

1. Department of Biological Sciences, Louisiana State University, Baton Rouge, Louisiana 70803, United States

2. Department of Experimental Statistics, Louisiana State University, Baton Rouge, Louisiana 70803, United States

3. Laboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Nagatsuta-cho, Yokohama, Kanagawa 226-8503, Japan

Funder

Institute of Innovative Research, Tokyo Institute of Technology

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.9b00272

Reference50 articles.

1. Deluca, M., and McElroy, W. D. (1978) Methods in Enzymology, Vol. 57, pp 3–15, Academic Press.

2. Functional regions of the cauliflower mosaic virus 35S RNA promoter determined by use of the firefly luciferase gene as a reporter of promoter activity

3. Use of firefly luciferase in atp-related assays of biomass, enzymes, and metabolites

4. Use of luciferase probes to measure ATP in living cells and animals

5. Demonstration of protein-fragment complementation assay using purified firefly luciferase fragments

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1. Correction to “Non-Steady State Analysis of Enzyme Kinetics in Real Time Elucidates Substrate Association and Dissociation Rates: Demonstration with Analysis of Firefly Luciferase Mutants”;Biochemistry;2024-03-12