EurekaMag.com logo
+ Site Statistics
References:
52,725,316
Abstracts:
28,411,598
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on Google+Follow on Google+
Follow on LinkedInFollow on LinkedIn

+ Translate

Covalent modification of Escherichia coli ADPglucose synthetase with 8-azido substrate analogs


Archives of Biochemistry and Biophysics 244(2): 585-595
Covalent modification of Escherichia coli ADPglucose synthetase with 8-azido substrate analogs
Two photoaffinity labeling agents, 8-azido-ATP and 8-azido-ADPglucose, are substrate site specific probes of the Escherichia coli ADPglucose synthetase. In the presence of light (254 nm), the analogs specifically and covalently modify the enzyme with concomitant loss of catalytic activity. The substrate ADPglucose completely protects the enzyme from covalent modification by these 8-azido analogs. ATP, another substrate, also provides nearly 100% protection from 8-azido-ATP inactivation but is less efficient in protection of inactivation by 8-azido-ADPglucose. In the absence of light, however, ADPglucose synthetase can utilize either 8-azido-ATP or 8-azido-ADPglucose as substrates.


Accession: 039703280

PMID: 3004345

DOI: 10.1016/0003-9861(86)90627-2



Related references

Covalent modification of substrate-binding sites of Escherichia coli ADP-glucose synthetase. Isolation and structural characterization of 8-azido-ADP-glucose-incorporated peptides. Journal of Biological Chemistry 261(3): 1058-1064, 1986

Covalent modification of the inhibitor-binding site(s) of Escherichia coli ADP-glucose synthetase. Isolation and structural characterization of 8-azido-AMP-incorporated peptides. Journal of Biological Chemistry 261(33): 15402-9, 1986

Covalent modification of the rec a protein from escherichia coli with the photoaffinity label 8 azido atp. Journal of Biological Chemistry 260(2): 867-872, 1985

GMP synthetase from Escherichia coli B-96. Interactions with substrate analogs. Biochimica et Biophysica Acta 370(2): 585-591, 1974

Gmp synthetase from escherichia coli strain b 96 interactions with substrate analogs. Biochimica et Biophysica Acta 370(2): 585-591, 1974

Regulation of glutamine synthetase activity and its biosynthesis in escherichia coli mediation by three cycles of covalent modification. Chock, P B , Et Al (Ed ) Enzyme Dynamics And Regulation; International Symposium on The Dynamics Of Soluble And Immobilized Enzyme Systems, Beijing, China, May 26-30, 1986 Xxi+421p Springer-Verlag: New York, New York, Usa; Berlin, West Germany Illus 136-145, 1988

Isoleucyl-tRNA synthetase from Escherichia coli MRE 600. Different pathways of the aminoacylation reaction depending on presence of pyrophosphatase, order of substrate addition in the pyrophosphate exchange, and substrate specificity with regard to ATP analogs. European Journal of Biochemistry 128(2-3): 315-329, 1982

In situ inactivation of escherichia coli uridylylation cycle is independent of the state of covalent modification of the components of the glutamine synthetase cascade. Archives of Biochemistry & Biophysics 219(2): 366-370, 1982

Mapping the aspartic acid binding site of Escherichia coli asparagine synthetase B using substrate analogs. Journal of Medicinal Chemistry 39(12): 2367-2378, 1996

The shikimate pathway part 4 3 dehydro quinate synthetase of escherichia coli substrate analogs and inhibitors. Biochimie (Paris) 58(9): 1145-1148, 1976