Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
SUBSTRATE-SPECIFICITY AND INHIBITOR SENSITIVITY OF CA2+ S100 DEPENDENT TWITCHIN KINASES/
Autore:
HEIERHORST J; TANG XX; LEI JY; PROBST WC; WEISS KR; KEMP BE; BENIAN GM;
Indirizzi:
ST VINCENTS INST MED RES,41 VICTORIA PARADE FITZROY VIC 3065 AUSTRALIA MT SINAI SCH MED,DEPT PHYSIOL & BIOPHYS NEW YORK NY 00000 EMORY UNIV,SCH MED,DEPT PATHOL & LAB MED ATLANTA GA 30322
Titolo Testata:
European journal of biochemistry
fascicolo: 3, volume: 242, anno: 1996,
pagine: 454 - 459
SICI:
0014-2956(1996)242:3<454:SAISOC>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
LIGHT CHAIN KINASE; CAENORHABDITIS-ELEGANS; MOLLUSCAN TWITCHIN; SYNTHETIC PEPTIDES; PROTEIN-KINASE; BASIC RESIDUES; PHOSPHORYLATION; SEQUENCE; LOCATION; PRODUCT;
Keywords:
PROTEIN KINASE; TWITCHIN; TITIN; S100; CALMODULIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
25
Recensione:
Indirizzi per estratti:
Citazione:
J. Heierhorst et al., "SUBSTRATE-SPECIFICITY AND INHIBITOR SENSITIVITY OF CA2+ S100 DEPENDENT TWITCHIN KINASES/", European journal of biochemistry, 242(3), 1996, pp. 454-459

Abstract

Myosin-associated giant protein kinases of the titin/twitchin-like superfamily have previously been implicated in the regulation of muscle function, based on genetic and physiological studies. We find that recombinant constitutively active Caenorhabditis elegans and Aplysia twitchin kinase fragments differ in their catalytic activities and peptide-substrate specificities, as well as in their sensitivities to the naphthalene sulfonamide inhibitors oronaphthalenesulfonyl)-1H-hexahydro-1,4-diazepine (ML-7) and odonaphthalenesulfonyl)-1H-hexahydro-1,4-diazepine (ML-9). The constitutively active Aplysia twitchin kinase fragment has a remarkably high activity (V-max > 100 mu mol . min(-1) . mg(-1)) towards some substrate peptides. The autoinhibited forms of these twitchin kinases can be activated in a Ca2+-dependent manner by the dimeric form of the S100A1 protein (S100A1(2)). The twitchin kinase S100A1(2)-binding site can also bind Ca2+/calmodulin but neither kinase is activated by calmodulin. The data provide a functional basis for the ongoing crystallographic study of twitchin kinase fragments.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 18:43:03