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Polyol-specific long-chain dehydrogenases/reductases of mannitol metabolism in Aspergillus fumigatus: biochemical characterization and pH studies of mannitol 2-dehydrogenase and mannitol-1-phosphate 5-dehydrogenase.
Chem Biol Interact. 2009 Mar 16; 178(1-3):274-82.CB

Abstract

Functional genomics data suggests that the metabolism of mannitol in the human pathogen Aspergillus fumigatus involves the action of two polyol-specific long-chain dehydrogenases/reductases, mannitol-1-phosphate 5-dehydrogenase (M1PDH) and mannitol 2-dehydrogenase (M2DH). The gene encoding the putative M2DH was expressed in Escherichia coli, and the purified recombinant protein was characterized biochemically. The predicted enzymatic function of a NAD(+)-dependent M2DH was confirmed. The enzyme is a monomer of 58kDa in solution and does not require metals for activity. pH profiles for M2DH and the previously isolated M1PDH were recorded in the pH range 6.0-10.0 for the oxidative and reductive direction of the reactions under conditions where substrate was limiting (k(cat)/K) or saturating (k(cat)). The pH-dependence of logk(cat) was usually different from that of log(k(cat)/K), suggesting that more than one step of the enzymatic mechanism was affected by changes in pH. The greater complexity of the pH profiles of log(k(cat)/K) for the fungal enzymes as compared to the analogous pH profiles for M2DH from Pseudomonas fluorescens may reflect sequence changes in vicinity of the conserved catalytic lysine.

Authors+Show Affiliations

Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, Graz, Austria.No 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

18983992

Citation

Krahulec, Stefan, et al. "Polyol-specific Long-chain Dehydrogenases/reductases of Mannitol Metabolism in Aspergillus Fumigatus: Biochemical Characterization and pH Studies of Mannitol 2-dehydrogenase and Mannitol-1-phosphate 5-dehydrogenase." Chemico-biological Interactions, vol. 178, no. 1-3, 2009, pp. 274-82.
Krahulec S, Armao GC, Bubner P, et al. Polyol-specific long-chain dehydrogenases/reductases of mannitol metabolism in Aspergillus fumigatus: biochemical characterization and pH studies of mannitol 2-dehydrogenase and mannitol-1-phosphate 5-dehydrogenase. Chem Biol Interact. 2009;178(1-3):274-82.
Krahulec, S., Armao, G. C., Bubner, P., Klimacek, M., & Nidetzky, B. (2009). Polyol-specific long-chain dehydrogenases/reductases of mannitol metabolism in Aspergillus fumigatus: biochemical characterization and pH studies of mannitol 2-dehydrogenase and mannitol-1-phosphate 5-dehydrogenase. Chemico-biological Interactions, 178(1-3), 274-82. https://doi.org/10.1016/j.cbi.2008.10.001
Krahulec S, et al. Polyol-specific Long-chain Dehydrogenases/reductases of Mannitol Metabolism in Aspergillus Fumigatus: Biochemical Characterization and pH Studies of Mannitol 2-dehydrogenase and Mannitol-1-phosphate 5-dehydrogenase. Chem Biol Interact. 2009 Mar 16;178(1-3):274-82. PubMed PMID: 18983992.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Polyol-specific long-chain dehydrogenases/reductases of mannitol metabolism in Aspergillus fumigatus: biochemical characterization and pH studies of mannitol 2-dehydrogenase and mannitol-1-phosphate 5-dehydrogenase. AU - Krahulec,Stefan, AU - Armao,Guilliano C, AU - Bubner,Patricia, AU - Klimacek,Mario, AU - Nidetzky,Bernd, Y1 - 2008/10/15/ PY - 2008/08/29/received PY - 2008/10/02/revised PY - 2008/10/03/accepted PY - 2008/11/6/pubmed PY - 2009/2/28/medline PY - 2008/11/6/entrez SP - 274 EP - 82 JF - Chemico-biological interactions JO - Chem. Biol. Interact. VL - 178 IS - 1-3 N2 - Functional genomics data suggests that the metabolism of mannitol in the human pathogen Aspergillus fumigatus involves the action of two polyol-specific long-chain dehydrogenases/reductases, mannitol-1-phosphate 5-dehydrogenase (M1PDH) and mannitol 2-dehydrogenase (M2DH). The gene encoding the putative M2DH was expressed in Escherichia coli, and the purified recombinant protein was characterized biochemically. The predicted enzymatic function of a NAD(+)-dependent M2DH was confirmed. The enzyme is a monomer of 58kDa in solution and does not require metals for activity. pH profiles for M2DH and the previously isolated M1PDH were recorded in the pH range 6.0-10.0 for the oxidative and reductive direction of the reactions under conditions where substrate was limiting (k(cat)/K) or saturating (k(cat)). The pH-dependence of logk(cat) was usually different from that of log(k(cat)/K), suggesting that more than one step of the enzymatic mechanism was affected by changes in pH. The greater complexity of the pH profiles of log(k(cat)/K) for the fungal enzymes as compared to the analogous pH profiles for M2DH from Pseudomonas fluorescens may reflect sequence changes in vicinity of the conserved catalytic lysine. SN - 1872-7786 UR - https://www.unboundmedicine.com/medline/citation/18983992/Polyol_specific_long_chain_dehydrogenases/reductases_of_mannitol_metabolism_in_Aspergillus_fumigatus:_biochemical_characterization_and_pH_studies_of_mannitol_2_dehydrogenase_and_mannitol_1_phosphate_5_dehydrogenase_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0009-2797(08)00544-9 DB - PRIME DP - Unbound Medicine ER -