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An endogenous proteinacious inhibitor in porcine liver for S-adenosyl-L-methionine dependent methylation reactions: identification as oligosaccharide-linked acyl carrier protein.

Authors
Seo, DW; Moon, HI; Han, JW; Hong, SY; Lee, HY; Kim, S; Paik, WK; Lee, HW
Citation
The international journal of biochemistry & cell biology, 32(4):455-464, 2000
Journal Title
The international journal of biochemistry & cell biology
ISSN
1357-27251878-5875
Abstract
A proteinacious inhibitor of S-adenosyl-L-methionine (AdoMet)-dependent transmethylation reactions was purified to homogeneity from porcine liver by size exclusion chromatography and FPLC. The molecular weight of the inhibitor was 12,222 Da. A 7400 Da polypeptide fragment of the purified inhibitor was sequenced by matrix-associated laser desorption ionization; time-of-flight MS, and was found to be identical with the known sequence of spinach acyl carrier protein (ACP). Although the remainder of the molecule was not clearly defined, 1H and H-H correlation of spectroscopy (COSY) NMR analysis revealed the presence of an oligosaccharide with alpha-glycosidic linkage. The purified oligosaccharide-linked ACP inhibited several AdoMet-dependent transmethylation reactions such as protein methylase I and II. S-farnesylcysteine O-methyltransferase, DNA methyltransferase and phospholipid methyltransferase. Protein methylase II was inhibited with a Ki value of 2.4 x 10(-3) M in a mixed inhibition pattern, whereas a well-known competitive product inhibitor S-adenosyl-L-homocysteine (AdoHcy) had Ki value of 6.3 x 10(-6) M. Commercially available active ACP fragments (65-74) and ACP from Escherichia coli had less inhibitory activity toward S-farnesylcysteine O-methyltransferase than the purified inhibitor. The biological significance of this oligosaccharide-linked ACP which has two seemingly unrelated functions (inhibitor for transmethylation and fatty acid biosynthesis) remains to be elucidated.
MeSH terms
Acyl Carrier Protein/*chemistry/isolation & purificationAnimalsEnzyme Inhibitors/chemistry/isolation & purificationKineticsLiver/*chemistryMagnetic Resonance SpectroscopyMethylationMethyltransferases/antagonists & inhibitors/chemistryMolecular WeightOligosaccharides/*chemistryPeptide Fragments/chemistryProtein Methyltransferases/chemistryRatsS-Adenosylmethionine/*chemistrySpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationSwineTransferases (Other Substituted Phosphate Groups)/chemistry
PMID
10762071
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Biochemistry & Molecular Biology
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