Physiological and biochemical characterization of AnNitA, the Aspergillus nidulans high-affinity nitrite transporter
| Autor: | Anthony D. M. Glass, Shiela E. Unkles, Ye Wang, James R. Kinghorn, Vicki F. Symington, Zorica Kotur, M. Yaeesh Siddiqi |
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| Rok vydání: | 2011 |
| Předmět: |
Models
Molecular Stereochemistry Kinetics Molecular Sequence Data Microbiology Aspergillus nidulans Protein Structure Secondary Fungal Proteins chemistry.chemical_compound Dry weight Asparagine Amino Acid Sequence Nitrite Molecular Biology Conserved Sequence Nitrites Fungal protein biology Membrane transport protein Cell Membrane Membrane Transport Proteins General Medicine Articles biology.organism_classification Protein Structure Tertiary Transmembrane domain chemistry Biochemistry Amino Acid Substitution biology.protein Mutagenesis Site-Directed |
| Zdroj: | Eukaryotic cell. 10(12) |
| ISSN: | 1535-9786 |
| Popis: | High-affinity nitrite influx into mycelia of Aspergillus nidulans has been characterized by use of 13 NO 2 − , giving average K m and V max values of 48 ± 8 μM and 228 ± 49 nmol mg −1 dry weight (DW) h −1 , respectively. Kinetic analysis of a plot that included an additional large number of low-concentration fluxes gave an excellent monophasic fit ( r 2 = 0.96), with no indication of sigmoidal kinetics. Two-dimensional (2D) and three-dimensional (3D) models of AnNitA are presented, and the possible roles of conserved asparagine residues N122 (transmembrane domain 3 ]Tm 3]), N173 (Tm 4), N214 (Tm 5), and N246 (Tm 6) are discussed. |
| Databáze: | OpenAIRE |
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