Services

Professional and Cost-Saving Solutions

Enzyme Activity Measurement for Pantetheine-Phosphate Adenylyltransferase



Creative Enzymes presents the most recent development and discoveries in enzyme activity assays. By constantly striving for services of utmost quality, Creative Enzymes has earned the trust of thousands of customers. We are specialized in highly customized and accurate bioanalytical services. Herein, we are glad to provide the most reliable enzymatic assay for pantetheine-phosphate adenylyltransferase.

Coenzyme A (CoA), the principal acyl-group carrier in all living cells, is required for numerous reactions in intermediary metabolism. CoA also plays a critical role in numerous biosynthetic, degradative, and energy-yielding metabolic pathways. In a living cell, CoA is synthesized from pantothenate (vitamin B5), cysteine, and ATP in five steps. Pantetheine-phosphate adenylyltransferase (EC 2.7.7.3; PPAT) catalyzes the penultimate step in this biosynthetic pathway by adenylating 4’-phosphopanthetheine to make dephospho-CoA. Subsequent phosphorylation at the 3’-hydroxyl of the ribose ring by dephospho-CoA kinase (EC 2.7.1.24) produces the acyl-group carrier, CoA. The rate of CoA biosynthesis is regulated by feedback inhibition of the first enzyme of the pathway, pantothenate kinase (EC 2.7.1.33). Studies of the intermediates of CoA biosynthesis have shown that both pantothenate and 4’-phosphopantetheine can accumulate in the cell, suggesting that PPAT may catalyze an additional rate-limiting step in the CoA biosynthesis pathway.

Enzyme Activity Measurement for Pantetheine-Phosphate Adenylyltransferase Figure 1: Biosynthesis of CoA in E. Coli.
Reference: Miller J R, et al. Journal of bacteriology, 2007, 189(22): 8196-8205.

PPAT is a member of the nucleotidyltransfer α/β phosphodiesterases family of enzymes, which transfer a nucleotide monophosphate moiety to other substrates. Bacterial PPATs are allosteric homohexamers. PPAT represents an attractive antibacterial target, since it catalyzes a key regulatory step in the CoA biosynthetic pathway and the human PPAT has distinct structures from its bacterial counterparts.

The activity of PPAT can be determined spectrophotometrically by a coupled assay. For instance, PPAT activity is assayed in the reverse direction using hexokinase and glucose-6-phosphate dehydrogenase to couple ATP production to NADP+ reduction. The assay is carried out at room temperature and the change in absorbance at 340 nm is monitored. The quality of our results is assured with the most advanced spectrophotometric instrument. We surpass our competitors with a quick assay turnover in response to the request of either a typical activity determination or a special need. Overall, Creative Enzymes is your trusty-worthy partner and looks forward to win your business as well.

Enzyme Activity Measurement for Pantetheine-Phosphate Adenylyltransferase Figure 2: The crystal structure of pantetheine-phosphate adenylyltransferase from E. Coli.
PDB: 1H1T



Inquiry
Related Products
CatalogEXWM-3240
EC No.EC 2.7.7.3
CAS No.9026-99-7
Source
CatalogNATE-1011
EC No.EC 2.7.7.3
CAS No.9026-99-7
SourceE. coli
Online Inquiry
Name:
*Phone:
*E-mail Address:
Country or Region:
Company/Institution:
*Products or Services of Interest:
Quantity:
Project Description:
Our products are not intended for private therapeutic use!
*Verification Code:
Please input "enzymes"(case insensitive) as verification code.

Welcome! For price inquiries, please feel free to contact us through the form on the left side. We will get back to you as soon as possible.


Sitemap | Privacy Policy | Terms and Conditions
Copyright ©2011 - 2019 Creative Enzymes.
Contact Us 45-1 Ramsey Road, Shirley, NY 11967, USA
Email: info@creative-enzymes.com
Tel: 1-631-562-8517 1-516-512-3133
Fax: 1-631-938-8127
Distributors To view the contact information for a specific location, select the desired country: