+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Isolation and various properties of nucleoside monophosphate kinases from Escherichia coli

Isolation and various properties of nucleoside monophosphate kinases from Escherichia coli

Prikladnaia Biokhimiia i Mikrobiologiia 24(3): 310-318

A technique is proposed for isolation of nucleosidemonophosphate kinases--AMP-kinase (EC, GMP-kinase (EC, CMP-kinase (EC, UMP-kinase (EC and TMP-kinase (EC E. coli MRE-600. It involves cell destroying, precipitation of nucleic acids with polyethyleneimine, fractionation with ammonium sulphate followed by chromatography on different carriers (DEAE-Toyopearl-650 M, Matrex gel Blue A, Matrex gel Red A). The technique enables all the five enzymes to be obtained separately and without contaminations with nucleotide dephosphorylating enzymes. For all the enzymes the pH optimum was found to range from 6.5 to 8.0, and Mg2+ ions were found to be the best activator for all the enzymes studied. The substrate specificity was investigated with respect to acceptors and donors of the phosphate groups. The enzymes showed strict specificity to the heterocyclic base of the acceptor phosphate group. AMP-, GMP- and CMP-kinases phosphorylated the corresponding deoxynucleoside monophosphates less effectively than ribonucleoside monophosphates. ATP was found to be the most effective phosphate donor for all the enzymes under study.

Please choose payment method:

(PDF emailed within 1 workday: $29.90)

Accession: 040520947

Download citation: RISBibTeXText

PMID: 2845390

Related references

Purification and some properties of nucleoside monophosphate kinases from escherichia coli. Prikladnaya Biokhimiya i Mikrobiologiya 244(3): 310-318, 1988

CMP kinase from Escherichia coli is structurally related to other nucleoside monophosphate kinases. Journal of Biological Chemistry 271(5): 2856-2862, 1996

Structure of Escherichia coli UMP kinase differs from that of other nucleoside monophosphate kinases and sheds new light on enzyme regulation. Journal of Biological Chemistry 280(27): 25533-25540, 2005

Nucleo-side monophosphate kinases II Transphosphorylation between adenosine monophosphate and nucleoside triphosphates. Biochimica et Biophysica Acta 32(none): 0-430, 1959

Multiplicity of adenosine 3',5'-monophosphate-dependent protein kinases from rat liver and mode of action of nucleoside 3',5'-monophosphate. Journal of Biological Chemistry 247(12): 3726-3735, 1972

Phosphorylation of nucleosides and nucleoside analogs by mammalian nucleoside monophosphate kinases. Pharmacology & Therapeutics 87(2-3): 189-198, 2000

The role of Ureaplasma nucleoside monophosphate kinases in the synthesis of nucleoside triphosphates. Febs Journal 274(8): 1983-1990, 2007

Nucleoside monophosphate kinases. I. Transphosphorylation between adenosine triphosphate and nucleoside monophosphates. Biochimica et Biophysica Acta 32: 412-421, 1959

Behavior of various ribo- and deoxyribonucleosides, nucleoside monophosphate kinases, and nucleoside diphosphokinase on Blue Sepharose affinity columns. Analytical Biochemistry 85(2): 425-429, 1978

Structures of Escherichia coli CMP kinase alone and in complex with CDP: A new fold of the nucleoside monophosphate binding domain and insights into cytosine nucleotide specificity. Structure 6(12): 1517-1527, 1998

Mycobacterium tuberculosis and Escherichia coli nucleoside diphosphate kinases lack multifunctional activities to process uracil containing DNA. Dna Repair 3(11): 1483-1492, 2004

Studies on pathogenic Escherichia coli isolated from chickens with colibacillosis. II. Antimicrobial drug resistance and transferable R plasmids in Escherichia coli. III. Biochemical properties and conjugal transfer of citrate-utilizing ability in citrate positive strains of Escherichia coli. IV. Isolation and characterization of R plasmid deoxyribonucleic acid. Korean Journal of Veterinary Public Health 8(1;2): 1-10, 15-19, 21-24, 1984

Isolation of nucleoside permeases from Escherichia coli. Advances in Experimental Medicine and Biology 309a: 439-442, 1991

Adenosine 3',5'-monophosphate-dependent protein kinases from mammalian artery: isolation and properties of the isoenzymes. Cellular and Molecular Biology Including Cyto-Enzymology 27(5): 419-428, 1981

Effect of mutations for adenylate cyclase (cya) and the cyclic adenosine monophosphate receptor protein (cgp) on the gene expression of nucleoside catabolism in Escherichia coli. Genetika 14(1): 103-110, 1978