Structure and enzymic reactivity of an aromatic five-membered cyclic phosphate diester. Biological implications

1971 ◽  
Vol 93 (9) ◽  
pp. 2351-2353 ◽  
Author(s):  
Emil T. Kaiser ◽  
Thomas W. S. Lee ◽  
F. Peter Boer
1979 ◽  
Vol 44 (2) ◽  
pp. 613-625 ◽  
Author(s):  
Valentina I. Gulyaeva ◽  
Antonín Holý

The present paper studies the effect of the modification of heterocyclic base, sugar moiety and the presence of phosphate group on the nucleoside acceptors in the synthesis of dinucleoside phosphates from adenosine 2',3'-cyclic phosphate as donor, catalyzed by nonspecific acidic extracellular and intracellular ribonucleases from Penicillium claviforme. The enzyme binds specifically the acceptor molecule, preferring cytosine nucleosides. It requires the presence of the whole sugar moiety, an exact mutual orientation of the heterocyclic base and the reaction center (5'-hydroxy group), and a suitable conformation of the acceptor molecule. The enzyme-acceptor bond is homochiral and the presence of the N3-H group in the pyrimidine ring is important. The reaction between the donor and the acceptor is bimolecular and is competitively inhibited by some purine nucleosides.


1980 ◽  
Vol 45 (2) ◽  
pp. 611-616 ◽  
Author(s):  
Antonina P. Kavunenko ◽  
Antonín Holý

Preparative synthesis of dinucleoside monophosphates, catalyzed by ribonuclease A, is described. Uridine 2',3' -cyclic phosphate was used as a donor, the acceptors being uridine (Ia), N3-methyl-uridine (Ib), 5-methyluridine (Ic), 6-methyluridine (Id), 3-(β-D-ribofuranosyl)uracil (IIa), 1-methyl-3-(β-D-ribofuranosyl)uracil (IIb), 6-azauridine (III) and 6-methyl-2'-deoxyuridine (IV). The obtained compounds of the type UpN (where N is the nucleoside moiety I-IV) were characterized by paper chromatography, electrophoresis and UV-spectra.


1987 ◽  
Vol 262 (1) ◽  
pp. 35-37
Author(s):  
R A Graham ◽  
R A Meyer ◽  
B S Szwergold ◽  
T R Brown

1995 ◽  
Vol 117 (37) ◽  
pp. 9441-9447 ◽  
Author(s):  
Mary Jane Young ◽  
Daphne Wahnon ◽  
Rosemary C. Hynes ◽  
Jik Chin
Keyword(s):  

1976 ◽  
Vol 54 (6) ◽  
pp. 834-837 ◽  
Author(s):  
Richard M. Epand ◽  
Connie Prosser

Exogenous cGMP can inhibit both basal and glucagon-stimulated production of glucose in liver slices from fed rats. Thus, cAMP and cGMP have opposite effects on the production of glucose in rat liver. Acetylcholine, an activator of guanylate cyclase (EC 4.6.1.2) in other systems, also inhibits the glucagon-stimulated production of glucose. No effect on glucose production was observed with secretin or exogenous GTP.


Sign in / Sign up

Export Citation Format

Share Document