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Characterization and purification of a membrane-bound archaebacterial pyrophosphatase from Sulfolobus acidocaldarius.
Eur J Biochem 1992; 207(2):741-6EJ

Abstract

Plasma membranes of the thermoacidophilic archaebacterium Sulfolobus acidocaldarius (DSM 639) display a pyrophosphate-hydrolyzing activity [M. Lübben & G. Schäfer (1987) Eur. J. Biochem. 164, 533-540]. In our present work, we solubilized and purified this pyrophosphatase to homogeneity. It consists of a single subunit with a molecular mass of 17-18 kDa, forming an oligomer of 70 kDa under native conditions. Edman degradation revealed 30 amino acids of the N-terminus. The enzyme cleaves phosphoric-acid-anhydride bonds independently of monovalent or divalent cations. Temperature and pH optima of 75 degrees C and 3.5-3.7, respectively, characterize it as an ectoenzyme. Membrane lipids of Sulfolobus stimulate the activity. The dolichol-pyrophosphate-complexing peptide-antibiotic bacitracin inhibited growth of Sulfolobus. A possible function of the acid pyrophosphatase is the hydrolysis of dolichol pyrophosphate in connection with glycosylation reactions of membrane proteins.

Authors+Show Affiliations

Institut für Biochemie, Medizinische Universität zu Lübeck, Federal Republic of Germany.No affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

1321720

Citation

Meyer, W, and G Schäfer. "Characterization and Purification of a Membrane-bound Archaebacterial Pyrophosphatase From Sulfolobus Acidocaldarius." European Journal of Biochemistry, vol. 207, no. 2, 1992, pp. 741-6.
Meyer W, Schäfer G. Characterization and purification of a membrane-bound archaebacterial pyrophosphatase from Sulfolobus acidocaldarius. Eur J Biochem. 1992;207(2):741-6.
Meyer, W., & Schäfer, G. (1992). Characterization and purification of a membrane-bound archaebacterial pyrophosphatase from Sulfolobus acidocaldarius. European Journal of Biochemistry, 207(2), pp. 741-6.
Meyer W, Schäfer G. Characterization and Purification of a Membrane-bound Archaebacterial Pyrophosphatase From Sulfolobus Acidocaldarius. Eur J Biochem. 1992 Jul 15;207(2):741-6. PubMed PMID: 1321720.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Characterization and purification of a membrane-bound archaebacterial pyrophosphatase from Sulfolobus acidocaldarius. AU - Meyer,W, AU - Schäfer,G, PY - 1992/7/15/pubmed PY - 1992/7/15/medline PY - 1992/7/15/entrez SP - 741 EP - 6 JF - European journal of biochemistry JO - Eur. J. Biochem. VL - 207 IS - 2 N2 - Plasma membranes of the thermoacidophilic archaebacterium Sulfolobus acidocaldarius (DSM 639) display a pyrophosphate-hydrolyzing activity [M. Lübben & G. Schäfer (1987) Eur. J. Biochem. 164, 533-540]. In our present work, we solubilized and purified this pyrophosphatase to homogeneity. It consists of a single subunit with a molecular mass of 17-18 kDa, forming an oligomer of 70 kDa under native conditions. Edman degradation revealed 30 amino acids of the N-terminus. The enzyme cleaves phosphoric-acid-anhydride bonds independently of monovalent or divalent cations. Temperature and pH optima of 75 degrees C and 3.5-3.7, respectively, characterize it as an ectoenzyme. Membrane lipids of Sulfolobus stimulate the activity. The dolichol-pyrophosphate-complexing peptide-antibiotic bacitracin inhibited growth of Sulfolobus. A possible function of the acid pyrophosphatase is the hydrolysis of dolichol pyrophosphate in connection with glycosylation reactions of membrane proteins. SN - 0014-2956 UR - https://www.unboundmedicine.com/medline/citation/1321720/Characterization_and_purification_of_a_membrane_bound_archaebacterial_pyrophosphatase_from_Sulfolobus_acidocaldarius_ L2 - https://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0014-2956&date=1992&volume=207&issue=2&spage=741 DB - PRIME DP - Unbound Medicine ER -