BROWSE

Related Researcher

Author's Photo

Kang, Byoung Heon
Cancer Biology Lab
Research Interests
  • Mitochondrial chaperones, cancer biology, cell death, metabolism, cancer stem cells, cancer therapeutics development

ITEM VIEW & DOWNLOAD

Inhibition studies on the nuclear inclusion protein a protease of turnip mosaic potyvirus C5

Cited 7 times inthomson ciCited 6 times inthomson ci
Title
Inhibition studies on the nuclear inclusion protein a protease of turnip mosaic potyvirus C5
Author
Kim, DHKang, Byoung HeonHwang, DCKim, SSKwon, TIChoi, KY
Issue Date
1996-12
Publisher
KOREAN SOC MOLECULAR & CELLULAR BIOLOGY
Citation
MOLECULES AND CELLS, v.6, no.6, pp.653 - 658
Abstract
The nuclear inclusion protein a (NIa) protease of turnip mosaic potyvirus is responsible for processing the viral precursor polyprotein into mature proteins. The NIa protease was found to be inhibited by several metal ions at micromolar concentrations, especially copper, zinc, and cadmium ions. This implies that the NIa protease may contain cysteine or histidine residues essential for the catalytic activity. Substitution of His-46 or Cys-151 to Tyr or Ser, respectively, abolished the catalytic activity almost completely, supporting the hypothesis that cysteine and histidine are involved in the catalysis. Nα-p-tosyl-L-phenylalanine chloromethylketone (TPCK) and Nα-p-tosyl-L-lysine chloromethylketone (TLCK) exhibited significant inhibitory effects on the catalytic activity of the NIa protease with IC50 values of 50 μM and 200 μM, respectively. This suggests chloromethylketone-conjugated peptides could work as potent inhibitors against NIa protease. Iodoacetamide, iodoacetate, and N-ethylmaleimide, which are known to modify cysteine or histidine, showed moderate inhibitory effects. The protease was inhibited negligibly by other serine or cysteine protease inhibitors such as leupeptin, antipain, aprotinin, phenylmethylsulfonyl fluoride, elastatinal, L-trans-epoxysuccinyl-leucylamido(4-guanidino)butane (E-64), and cystatin. These results suggest that although the active site of the NIa protease is structurally similar to that of the chymotrypsin-like serine protease, it has a unique active site specificity distinct from those of other serine proteases.
URI
https://scholarworks.unist.ac.kr/handle/201301/7133
URL
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0010565668
ISSN
1016-8478
Appears in Collections:
BIO_Journal Papers
Files in This Item:
There are no files associated with this item.

find_unist can give you direct access to the published full text of this article. (UNISTARs only)

Show full item record

qrcode

  • mendeley

    citeulike

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

MENU