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Titolo:
THE ATPASE ACTIVITY OF PURIFIED CDC48P FROM SACCHAROMYCES-CEREVISIAE SHOWS COMPLEX DEPENDENCE ON ATP-CONCENTRATION, ADP-CONCENTRATION, AND NADH-CONCENTRATION AND IS COMPLETELY INHIBITED BY NEM
Autore:
FROHLICH KU; FRIES HW; PETERS JM; MECKE D;
Indirizzi:
INST PHYSIOL CHEM,HOPPE SEYLER STR 4 D-72076 TUBINGEN GERMANY DEUTSCH KREBSFORSCHUNGSZENTRUM,ZELLBIOL ABT D-69120 HEIDELBERG GERMANY
Titolo Testata:
Biochimica et biophysica acta. Protein structure and molecular enzymology
fascicolo: 1, volume: 1253, anno: 1995,
pagine: 25 - 32
SICI:
0167-4838(1995)1253:1<25:TAAOPC>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
PEROXISOME BIOGENESIS; VESICULAR TRANSPORT; ESCHERICHIA-COLI; BINDING PROTEIN; GENE; YEAST; FUSION; MEMBER; FAMILY; VCP;
Keywords:
CDC48P PROTEIN; ATPASE ACTIVITY; INHIBITION; CELL CYCLE PROTEIN; N-ETHYLMALEIMIDE; (S-CERVISIAE);
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
K.U. Frohlich et al., "THE ATPASE ACTIVITY OF PURIFIED CDC48P FROM SACCHAROMYCES-CEREVISIAE SHOWS COMPLEX DEPENDENCE ON ATP-CONCENTRATION, ADP-CONCENTRATION, AND NADH-CONCENTRATION AND IS COMPLETELY INHIBITED BY NEM", Biochimica et biophysica acta. Protein structure and molecular enzymology, 1253(1), 1995, pp. 25-32

Abstract

The cell cycle protein CDC48p from Saccharomyces cerevisiae is a member of a protein superfamily (AAA superfamily) characterized by a common region of approximately 200 amino-acid residues including an ATP binding consensus. CDC48p purified to homogeneity showed considerable ATPase activity which could be completely abolished by preincubation withNEM in the absence of ATP. ATP protects the protein from NEM and stabilizes the otherwise labile enzyme. The ATPase activity is reversibly inhibited by NADH and shows cooperativity with its substrate ATP. The application of the in vitro ATPase activity to the identification of physiologically interacting molecules is discussed. By electron microscopy, the enzyme was shown to consist of hexameric ring structures similar to its vertebrate homologue.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/07/20 alle ore 22:19:32