Tags

Type your tag names separated by a space and hit enter

An ecto-enzyme from Sulfolobus acidocaldarius strain 7 which catalyzes hydrolysis of inorganic pyrophosphate, ATP, and ADP: purification and characterization.
J Biochem 1993; 114(3):329-33JB

Abstract

Membranes of Sulfolobus acidocaldarius, a thermoacidophilic archaebacterium, show novel enzymatic activities to hydrolyze PPi, ATP, and ADP at an optimal pH of 3, equal to the growth optimum. The activity increased by about 2-fold on addition of PPi and/or Pi to the growth medium, when yeast extract and casamino acids were removed. The enzyme which hydrolyzes PPi at pH 3 was solubilized and purified by successive chromatographies. The final preparation showed a 26 kDa single band on SDS-PAGE, and a molecular mass of 35 kDa on gel permeation chromatography. The Km and Vmax for PPi were 0.16 mM and 33 mumol Pi released/min/mg at 55 degrees C. ATP and ADP were also good substrates. Divalent cations were not essential for activity. Substrate inhibition at more than 5 mM PPi, ATP or ADP was observed. AMP, glucose-6-phosphate, and p-nitrophenyl phosphate were not hydrolyzed at all. The activity was 4-fold stimulated by addition of the lipid fraction extracted from the organism.

Authors+Show Affiliations

Department of Life Science and Bioengineering, Tokyo Institute of Technology, Yokohama.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

8282721

Citation

Amano, T, et al. "An Ecto-enzyme From Sulfolobus Acidocaldarius Strain 7 Which Catalyzes Hydrolysis of Inorganic Pyrophosphate, ATP, and ADP: Purification and Characterization." Journal of Biochemistry, vol. 114, no. 3, 1993, pp. 329-33.
Amano T, Wakagi T, Oshima T. An ecto-enzyme from Sulfolobus acidocaldarius strain 7 which catalyzes hydrolysis of inorganic pyrophosphate, ATP, and ADP: purification and characterization. J Biochem. 1993;114(3):329-33.
Amano, T., Wakagi, T., & Oshima, T. (1993). An ecto-enzyme from Sulfolobus acidocaldarius strain 7 which catalyzes hydrolysis of inorganic pyrophosphate, ATP, and ADP: purification and characterization. Journal of Biochemistry, 114(3), pp. 329-33.
Amano T, Wakagi T, Oshima T. An Ecto-enzyme From Sulfolobus Acidocaldarius Strain 7 Which Catalyzes Hydrolysis of Inorganic Pyrophosphate, ATP, and ADP: Purification and Characterization. J Biochem. 1993;114(3):329-33. PubMed PMID: 8282721.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - An ecto-enzyme from Sulfolobus acidocaldarius strain 7 which catalyzes hydrolysis of inorganic pyrophosphate, ATP, and ADP: purification and characterization. AU - Amano,T, AU - Wakagi,T, AU - Oshima,T, PY - 1993/9/1/pubmed PY - 1993/9/1/medline PY - 1993/9/1/entrez SP - 329 EP - 33 JF - Journal of biochemistry JO - J. Biochem. VL - 114 IS - 3 N2 - Membranes of Sulfolobus acidocaldarius, a thermoacidophilic archaebacterium, show novel enzymatic activities to hydrolyze PPi, ATP, and ADP at an optimal pH of 3, equal to the growth optimum. The activity increased by about 2-fold on addition of PPi and/or Pi to the growth medium, when yeast extract and casamino acids were removed. The enzyme which hydrolyzes PPi at pH 3 was solubilized and purified by successive chromatographies. The final preparation showed a 26 kDa single band on SDS-PAGE, and a molecular mass of 35 kDa on gel permeation chromatography. The Km and Vmax for PPi were 0.16 mM and 33 mumol Pi released/min/mg at 55 degrees C. ATP and ADP were also good substrates. Divalent cations were not essential for activity. Substrate inhibition at more than 5 mM PPi, ATP or ADP was observed. AMP, glucose-6-phosphate, and p-nitrophenyl phosphate were not hydrolyzed at all. The activity was 4-fold stimulated by addition of the lipid fraction extracted from the organism. SN - 0021-924X UR - https://www.unboundmedicine.com/medline/citation/8282721/An_ecto_enzyme_from_Sulfolobus_acidocaldarius_strain_7_which_catalyzes_hydrolysis_of_inorganic_pyrophosphate_ATP_and_ADP:_purification_and_characterization_ L2 - https://joi.jlc.jst.go.jp/JST.Journalarchive/biochemistry1922/114.329?lang=en&from=PubMed DB - PRIME DP - Unbound Medicine ER -