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Reference on EC 3.2.2.4 - AMP nucleosidase

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Giranda, V.L.; Berman, H.M.; Schramm, V.L.
Crystallographic quaternary structural analysis of AMP nucleosidases from Escherichia coli and Azotobacter vinelandii
J. Biol. Chem.
264
15674-15680
1989
Azotobacter vinelandii, Escherichia coli
Manually annotated by BRENDA team
Giranda, V.L.; Berman, H.M.; Schramm, V.L.
Crystal structure of formycin 5'-phosphate: An explanation for its tight binding to AMP nucleosidase
Biochemistry
27
5813-5818
1988
Azotobacter vinelandii, Escherichia coli
Manually annotated by BRENDA team
Leung, H.B.; Schramm, V.L.
The structural gene for AMP nucleosidase. Mapping, cloning, and overproduction of the enzyme
J. Biol. Chem.
259
6972-6978
1984
Azotobacter vinelandii, Escherichia coli
Manually annotated by BRENDA team
Giranda, V.L.; Berman, H.M.; Schramm, V.L.
Crystallization and preliminary X-ray study of AMP nucleosidase
J. Biol. Chem.
261
15307-15309
1986
Azotobacter vinelandii, Escherichia coli
Manually annotated by BRENDA team
Parkin, D.W.; Schramm, V.L.
Catalytic and allosteric mechanism of AMP nucleosidase from primary, beta-secondary, and multiple heavy atom kinetic isotope effects
Biochemistry
26
913-920
1987
Azotobacter vinelandii, Escherichia coli
Manually annotated by BRENDA team
Mentch, F.; Parkin, D.W.; Schramm, V.L.
Transition state structures for N-glycoside hydrolysis of AMP by acid and by AMP nucleosidase in the presence and absence of allosteric activator
Biochemistry
26
921-930
1987
Azotobacter vinelandii
Manually annotated by BRENDA team
DeWolf, W.E.; Emig, F.A.; Schramm, V.L.
AMP nucleosidase: Kinetic mechanism and thermodynamics
Biochemistry
25
4132-4140
1986
Azotobacter vinelandii
Manually annotated by BRENDA team
Skoog, M.T.
Mechanism and activation for allosteric adenosine 5-monophosphate nucleosidase
J. Biol. Chem.
261
4451-4459
1986
Azotobacter vinelandii
Manually annotated by BRENDA team
Parkin, D.W.; Schramm, V.L.
Effects of allosteric activation on the primary and secondary kinetic isotope effects for three AMP nucleosidases
J. Biol. Chem.
259
9418-9425
1984
Azotobacter vinelandii, Escherichia coli
Manually annotated by BRENDA team
Marriott, I.D.; Dawes, E.A.; Rowley, B.I.
Effect of growth rate and nutrient limitation on the adenine nucleotide content, energy charge and enzymes of adenylate metabolism in Azotobacter beijerinckii
J. Gen. Microbiol.
125
375-382
1981
Azotobacter vinelandii, Azotobacter beijerinckii
-
Manually annotated by BRENDA team
Yoshino, M.; Tsukada, T.; Muratami, K.; Tsushima, K.
Adenine nucleotide metabolism in Azotobacter vinelandii. Two metabolic pathways of AMP degradation
Arch. Microbiol.
128
222-227
1980
Azotobacter vinelandii
Manually annotated by BRENDA team
Parkin, D.W.; Mentch, F.; Banks, G.A.; Horenstein, B.A.; Schramm, V.L.
Transition-state analysis of a Vmax mutant of AMP nucleosidase by the application of heavy-atom kinetic isotope effects
Biochemistry
30
4586-4594
1991
Azotobacter vinelandii
Manually annotated by BRENDA team
Leung, H.B.; Kvalnes-Krick, K.L.; Meyer, S.L.; deRiel, J.K.; Schramm, V.L.
Structure and regulation of the AMP nucleosidase gene (amn) from Escherichia coli
Biochemistry
28
8726-8733
1989
Azotobacter vinelandii, Escherichia coli
Manually annotated by BRENDA team
Leung, H.B.; Schramm, V.L.
A mutant AMP nucleosidase. Purification, properties and in vivo turnover of the protein
J. Biol. Chem.
256
12823-12829
1981
Azotobacter vinelandii
Manually annotated by BRENDA team
Leung, H.B.; Schramm, V.L.
Adenylate degradation in Escherichia coli. The role of Amp nucleosidase and properties of the purified enzyme
J. Biol. Chem.
255
10867-10874
1980
Escherichia coli
Manually annotated by BRENDA team
De Wolf Jr., W.E.; Markham, G.D.; Schramm, V.L.
Evidence for substantial separation of the catalytic and allosteric sites of AMP nucleosidase
J. Biol. Chem.
255
8210-8215
1980
Azotobacter vinelandii
Manually annotated by BRENDA team
Schramm, V.L.; Reed, G.H.
Interaction of Mn2+ and MnATP2- with the allosteric sites of AMP nucleosidase
J. Biol. Chem.
255
5795-5801
1980
Azotobacter vinelandii
-
Manually annotated by BRENDA team
Murakami, K.; Yoshino, M.
Ion-dependent activation of AMP nucleosidase from Azotobacter vinelandii
Biochim. Biophys. Acta
613
153-159
1980
Azotobacter vinelandii
Manually annotated by BRENDA team
Yoshino, M.; Murakami, K.; Tsushima, K.
Effects of monovalent cations on AMP nucleosidase from Azotobacter vinelandii
Biochim. Biophys. Acta
570
118-123
1979
Azotobacter vinelandii
Manually annotated by BRENDA team
Yoshino, M.; Murakami, K.; Tsushima, K.
Polyamines as activators of AMP nucleosidase from Azotobacter vinelandii
Experientia
35
587-579
1979
Azotobacter vinelandii
-
Manually annotated by BRENDA team
Schramm, V.L.; Hochstein, L.I.
Stabilization of allosteric adenosine monophosphate nucleosidase by inorganic salts, substrate, and essential activator
Biochemistry
10
3411-3417
1971
Azotobacter vinelandii
Manually annotated by BRENDA team
DeWolf Jr., W.E.; Fullin, F.A.; Schramm, V.L.
The catalytic site of AMP nucleosidase
J. Biol. Chem.
254
10868-10875
1979
Azotobacter vinelandii
Manually annotated by BRENDA team
DeWolf Jr., W.E.; Schramm, V.L.
Synthesis of a new 8-spin-labeled analog of adenosine 5-phosphate and its interaction with AMP nucleosidase
J. Biol. Chem.
254
6215-6217
1979
Azotobacter vinelandii
Manually annotated by BRENDA team
Schramm, V.L.; Leung, H.B.
Adenosine monophosphate nucleosidase from Azotobacter vinelandii and Escherichia coli
Methods Enzymol.
33
263-271
1978
Azotobacter vinelandii, Escherichia coli
Manually annotated by BRENDA team
Hurwitz, J.; Heppel, L.A.; Horecker, B.L.
The enzymatic cleavage of adenylic acid to adenine and ribose 5-phosphate
J. Biol. Chem.
226
525-540
1957
Azotobacter vinelandii
Manually annotated by BRENDA team
Yoshino, M.; Murakami, K.; Tsushima, K.
Flavodoxin: An allosteric inhibitor of AMP nucleosidase from Azotobacter vinelandii
J. Biochem.
80
839-843
1976
Azotobacter vinelandii
Manually annotated by BRENDA team
Yoshino, M.
AMP nucleosidase from Azotobacter vinelandii
J. Biochem.
68
321-329
1970
Azotobacter vinelandii
Manually annotated by BRENDA team
Ogasawara, N.; Yoshino, M.; Asai, J.
AMP nucleosidase from Azotobacter vinelandii
J. Biochem.
68
331-340
1970
Azotobacter vinelandii
Manually annotated by BRENDA team
Schramm, V.L.; Fullin, F.A.
Kinetics of adenosine monophosphate nucleosidase inactivation by phosphate and protection by substrate and allosteric activator
J. Biol. Chem.
253
2161-2167
1978
Azotobacter vinelandii
Manually annotated by BRENDA team
Schramm, V.L.
Comparison of initial velocity and binding data for allosteric adenosine monophosphate nucleosidase
J. Biol. Chem.
251
3417-3424
1976
Azotobacter vinelandii
Manually annotated by BRENDA team
Schramm, V.L.
Kinetic properties of allosteric adenosine monophosphate nucleosidase from Azotobacter vinelandii
J. Biol. Chem.
249
1729-1736
1974
Azotobacter vinelandii
Manually annotated by BRENDA team
Yoshino, M.; Takagi, T.
Subunit structure of AMP nucleosidase from Azotobacter vinelandii
J. Biochem.
74
1151-1156
1973
Azotobacter vinelandii
Manually annotated by BRENDA team
Schramm, V.L.; Hochstein, L.I.
Purification, crystallization, and subunit structure of allosteric adenosine 5-monophosphate nucleosidase
Biochemistry
11
2777-2783
1972
Azotobacter vinelandii
Manually annotated by BRENDA team
Yoshino, M.; Ogasawara, N.; Suzuki, N.; Kotake, Y.
Regulation of AMP nucleosidase in Azotobacter vinelandii
Biochim. Biophys. Acta
146
620-622
1967
Azotobacter vinelandii
Manually annotated by BRENDA team
Ehrlich, J.I.; Schramm, V.L.
Electrostatic potential surface analysis of the transition state for AMP nucleosidase and for formycin 5'-phosphate, a transition state inhibitor
Biochemistry
33
8890-8896
1994
Azotobacter vinelandii
Manually annotated by BRENDA team
Zhang, Y.; Cottet, S.E.; Ealick, S.E.
Structure of Escherichia coli AMP nucleosidase reveals similarity to nucleoside phosphorylases
Structure
12
1383-1394
2004
Escherichia coli
Manually annotated by BRENDA team
Morrison, B.A.; Shain, D.H.
An AMP nucleosidase gene knockout in Escherichia coli elevates intracellular ATP levels and increases cold tolerance
Biol. Lett.
4
53-56
2008
Escherichia coli
Manually annotated by BRENDA team
Bujara, M.; Schuemperli, M.; Billerbeck, S.; Heinemann, M.; Panke, S.
Exploiting cell-free systems: Implementation and debugging of a system of biotransformations
Biotechnol. Bioeng.
106
376-389
2010
Escherichia coli, Escherichia coli W3110 / ATCC 27325
Manually annotated by BRENDA team