[Analogs of 3'-dephospho-CoASH with a phosphodiester bond as substrates of the S-acetylation reaction, catalyzed by acetyl-CoA-synthetase fom rabbit myocardium].
A number of earlier unknown 3'-dephospho-CoASH analogues with the pyrophosphate fragment replaced by an ester or phosphodiester bond were synthesized and tested in S-acetylation reaction, catalyzed by acetyl-CoA synthetase (EC 6.2.1.1) from rabbit myocardium. 3'-Dephospho-CoASH analogues with a phosphodiester bond, e.g. (Ia), had a lower affinity and diminished kinetic parameters than 3'-dephospho-CoASH (Km = 1 and 0.2 mM, respectively). The adenine substitution in (Ia) by guanine or hypoxanthine (but not cytosine) residue resulted in a loss of substrate properties. 3'-Dephospho-CoASH with an ester bond were not capable of accepting acetate under conditions used and only slightly inhibited the enzymic activity.
Biriukov
A I
AI
Zhukov
Iu N
IuN
Kopelevich
V M
VM
Bulanova
L N
LN
Gunar
V I
VI
D000106:Acetate-CoA Ligase / Q000378:metabolism*; D000107:Acetylation; D000818:Animals; D002384:Catalysis; D003065:Coenzyme A / Q000737:chemistry / Q000378:metabolism*; D004952:Esters / Q000737:chemistry; D007700:Kinetics; D009206:Myocardium / Q000201:enzymology*; D009943:Organophosphorus Compounds / Q000737:chemistry*; D011817:Rabbits; D013379:Substrate Specificity
D004952:Esters; D009943:Organophosphorus Compounds; C015787:dephosphocoenzyme A; D000106:Acetate-CoA Ligase; D003065:Coenzyme A
Analogi 3'-defosfo-CoASH s fosfodiéfirnoĭ sviaz'iu kak substraty reaktsii S-atsetilirovaniia, kataliziruemoĭ atsetil-CoA-sintetazoĭ miokarda krolika.