Is there 'dolichol recognition sequence' in enzymes that interact with dolichols and other polyisoprenoid substrates ?

• Autorzy: Schutzbach J. S.
• Języki publikacji: EN

Abstrakty

Yeas t dolichyl-P-mannose synthase and a number of other enzymes that interact with dolichol or dolichyl-P as substrates contain a highly conserved amino-acid sequence that has been proposed as a potential dolichol recognition sequence [Albright, C.F., Orlean, P. & Robbins, P.W. (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 7366-7369]. In dolichyl-P-mannose synthase/ the most highly conserved amino-acid residues of this domain were modified by site directed mutagenesis, and for one construct the sequence was completely deleted. Enzymes containing the site directed modifications/ and the deletion mutant, were found to retain catalytic activity, and all of the modified enzymes had the same apparent affinity for Dol-P as wild type enzyme when assayed in a phospholipid matrix. Based on these results, the amino-acid composition and sequence of the conserved domain are not critically important for the recognition and binding of Dol-P when the synthase is reconstituted in a lipid matrix.

Słowa kluczowe

EN

enzyme; recognition sequence; dolichol-P-mannose; polyisoprenoid substrate; synthase

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1994
• Tom: 41
• Numer: 3
• Opis fizyczny: p.270-274,fig.

Twórcy

autor

Schutzbach J. S.

• University of Alabama at Birmingham, Birmingham, AL 35294-0019, USA

Bibliografia

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