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On the biochemical classification of yeast trehalases: Candida albicans contains two enzymes with mixed features of neutral and acid trehalase activities.
Biochem Biophys Res Commun. 2009 May 22; 383(1):98-102.BB

Abstract

Two enzymes endowed with trehalase activity are present in Candida albicans. The cytosolic trehalase (Ntc1p), displayed high activity in exponential phase regardless of the carbon source (glucose, trehalose or glycerol). Ntc1p activity was similar in neutral (pH 7.1) or acid (pH 4.5) conditions, strongly inhibited by ATP, weakly stimulated by divalent cations (Ca(2+)or Mn(2+)) and unaffected in the presence of cyclic AMP. The Ntc1p activity decreased in stationary phase, except in glycerol-grown cultures, but the catalytic properties did not change. In turn, the cell wall-linked trehalase (Atc1p) showed elevated activity in resting cells or in cultures growing on trehalose or glycerol. Although Atc1p is subjected to glucose repression, exhaustion of glucose in itself did not increased the activity. Significant Atc1p values could also be measured at neutral or acid pH, but Atc1p was insensitive to ATP, cyclic AMP and divalent cations. These results are in direct contrast with the current classification of yeast trehalases based on their optimum pH. They are also relevant in the light of the proposed use of trehalase inhibitors for the treatment of candidiasis.

Authors+Show Affiliations

Universidad de Murcia, Spain.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

19336219

Citation

Sánchez-Fresneda, Ruth, et al. "On the Biochemical Classification of Yeast Trehalases: Candida Albicans Contains Two Enzymes With Mixed Features of Neutral and Acid Trehalase Activities." Biochemical and Biophysical Research Communications, vol. 383, no. 1, 2009, pp. 98-102.
Sánchez-Fresneda R, González-Párraga P, Esteban O, et al. On the biochemical classification of yeast trehalases: Candida albicans contains two enzymes with mixed features of neutral and acid trehalase activities. Biochem Biophys Res Commun. 2009;383(1):98-102.
Sánchez-Fresneda, R., González-Párraga, P., Esteban, O., Laforet, L., Valentín, E., & Argüelles, J. C. (2009). On the biochemical classification of yeast trehalases: Candida albicans contains two enzymes with mixed features of neutral and acid trehalase activities. Biochemical and Biophysical Research Communications, 383(1), 98-102. https://doi.org/10.1016/j.bbrc.2009.03.134
Sánchez-Fresneda R, et al. On the Biochemical Classification of Yeast Trehalases: Candida Albicans Contains Two Enzymes With Mixed Features of Neutral and Acid Trehalase Activities. Biochem Biophys Res Commun. 2009 May 22;383(1):98-102. PubMed PMID: 19336219.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - On the biochemical classification of yeast trehalases: Candida albicans contains two enzymes with mixed features of neutral and acid trehalase activities. AU - Sánchez-Fresneda,Ruth, AU - González-Párraga,Pilar, AU - Esteban,Oscar, AU - Laforet,Leslie, AU - Valentín,Eulogio, AU - Argüelles,Juan-Carlos, Y1 - 2009/03/29/ PY - 2009/03/23/received PY - 2009/03/24/accepted PY - 2009/4/2/entrez PY - 2009/4/2/pubmed PY - 2009/5/20/medline SP - 98 EP - 102 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 383 IS - 1 N2 - Two enzymes endowed with trehalase activity are present in Candida albicans. The cytosolic trehalase (Ntc1p), displayed high activity in exponential phase regardless of the carbon source (glucose, trehalose or glycerol). Ntc1p activity was similar in neutral (pH 7.1) or acid (pH 4.5) conditions, strongly inhibited by ATP, weakly stimulated by divalent cations (Ca(2+)or Mn(2+)) and unaffected in the presence of cyclic AMP. The Ntc1p activity decreased in stationary phase, except in glycerol-grown cultures, but the catalytic properties did not change. In turn, the cell wall-linked trehalase (Atc1p) showed elevated activity in resting cells or in cultures growing on trehalose or glycerol. Although Atc1p is subjected to glucose repression, exhaustion of glucose in itself did not increased the activity. Significant Atc1p values could also be measured at neutral or acid pH, but Atc1p was insensitive to ATP, cyclic AMP and divalent cations. These results are in direct contrast with the current classification of yeast trehalases based on their optimum pH. They are also relevant in the light of the proposed use of trehalase inhibitors for the treatment of candidiasis. SN - 1090-2104 UR - https://www.unboundmedicine.com/medline/citation/19336219/On_the_biochemical_classification_of_yeast_trehalases:_Candida_albicans_contains_two_enzymes_with_mixed_features_of_neutral_and_acid_trehalase_activities_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(09)00620-2 DB - PRIME DP - Unbound Medicine ER -