NDLI: 2'-Phosphoadenylylation of eukaryotic proteins: a type of covalent modification.

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2'-Phosphoadenylylation of eukaryotic proteins: a type of covalent modification.

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2'-Phosphoadenylylation of eukaryotic proteins: a type of covalent modification.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Klapproth, K. Hilz, H. Fanick, W.
Abstract	An enzymatic system in rat liver microsomal preparations has been detected that catalyzes the transfer of the 2'-phospho-AMP moiety from NADP to endogenous polypeptides; the major acceptor is a polypeptide of about 40 kDa (p40). Modification of the acceptor by 2'-phospho-AMP residues was deduced from the simultaneous transfer of 2'-[33P]phosphate and [3H]adenine residues from double-labeled NADP, while no incorporation of radioactivity into p40 was seen with NADP species labeled in the NMN moiety. The true substrate of this phosphoadenylylation reaction was 2'-phospho-ADP-ribose rather than NADP, because labeled phospho-ADP-ribose was as efficient as or more efficient than NADP in forming modified p40. Also, NADP was rapidly converted to phospho-ADP-ribose during incubation with microsomes. Furthermore, isonicotinic acid hydrazide, an inhibitor of NADP glycohydrolase, prevented phosphoadenylylation from NADP, but not from phospho-ADP-ribose, and glycohydrolase-resistant NADPH could not substitute for NADP. Transferase activity was found in liver and brain microsomes and, to a smaller extent, in the cytosol fractions. In Ehrlich ascites tumor cells, most of the activity resided in the cytosol, from which it could be partially purified. The apparent Km for phospho-ADP-ribose was about 2 X 10(-4) M, and the pH optimum was around 7. Divalent cations like Mg2+ and Mn2+ inhibited the reaction. In all compartmental preparations, activity was eliminated by heating or short treatment with alkali or acid. In submitochondrial particles from rat liver, a system with different characteristics led to the phosphoadenylylation of several endogenous polypeptides.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	17
Volume Number	83
Language	English
Publisher	National Academy of Sciences
Publisher Date	1986-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Adenosine Diphosphate Ribose Analogs & Derivatives Microsomes, Liver Metabolism NADP Nucleoside Diphosphate Sugars Phosphoproteins Protein Processing, Post-Translational Adenosine Monophosphate Animals Cell Compartmentation Chemical Phenomena Chemistry Molecular Weight Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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