scholarly journals Crystal structure of Aspergillus fumigatus AroH , an aromatic amino acid aminotransferase

2021 ◽  
Author(s):  
Sharon Spizzichino ◽  
Gioena Pampalone ◽  
Mirco Dindo ◽  
Agostino Bruno ◽  
Luigina Romani ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Aspergillus Fumigatus ◽  
Aromatic Amino Acid ◽  
Aromatic Amino Acid Aminotransferase

scholarly journals Biochemical Characterization of Aspergillus fumigatus AroH, a Putative Aromatic Amino Acid Aminotransferase

2018 ◽  
Vol 5 ◽  
Author(s):  
Mirco Dindo ◽  
Egidia Costanzi ◽  
Marco Pieroni ◽  
Claudio Costantini ◽  
Giannamaria Annunziato ◽  
...  
Keyword(s):  
Amino Acid ◽  
Aspergillus Fumigatus ◽  
Aromatic Amino Acid ◽  
Biochemical Characterization ◽  
Aromatic Amino Acid Aminotransferase

scholarly journals Crystal structure of the aromatic-amino-acid aminotransferase fromStreptococcus mutans

2019 ◽  
Vol 75 (2) ◽  
pp. 141-146
Author(s):  
Xuzhen Cong ◽  
Xiaolu Li ◽  
Shentao Li
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Streptococcus Mutans ◽  
Aromatic Amino Acid ◽  
Aromatic Amino Acids ◽  
Diffusion Method ◽  
Molecular Replacement ◽  
Replacement Method ◽  
Molecular Replacement Method ◽  
Aromatic Amino Acid Aminotransferase

Streptococcus mutans, a facultatively aerobic and Gram-positive bacterium, is the primary causative agent of dental caries and contributes to the multispecies biofilm known as dental plaque. In this study, the aromatic-amino-acid aminotransferase fromStreptococcus mutans(SmAroAT) was recombinantly expressed inEscherichia coli. An effective purification protocol was established. The recombinant protein was crystallized using the hanging-drop vapor-diffusion method with PEG 3350 as the primary precipitant. The crystal structure ofSmAroAT was solved at 2.2 Å resolution by the molecular-replacement method. Structural analysis indicated that the proteins of the aromatic-amino-acid aminotransferase family have conserved structural elements that might play a role in substrate binding. These results may help in obtaining a better understanding of the catabolism and biosynthesis of aromatic amino acids.

Escherichia coli aromatic amino acid aminotransferase: Characterization and comparison with aspartate aminotransferase

Biochemistry ◽  
1993 ◽  
Vol 32 (45) ◽  
pp. 12229-12239 ◽  
Author(s):  
Hideyuki Hayashi ◽  
Katsura Inoue ◽  
Toshihito Nagata ◽  
Seiki Kuramitsu ◽  
Hiroyuki Kagamiyama
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Aspartate Aminotransferase ◽  
Aromatic Amino Acid ◽  
Aromatic Amino Acid Aminotransferase

scholarly journals Histidine Degradation via an Aminotransferase Increases the Nutritional Flexibility of Candida glabrata

2014 ◽  
Vol 13 (6) ◽  
pp. 758-765 ◽  
Author(s):  
Sascha Brunke ◽  
Katja Seider ◽  
Martin Ernst Richter ◽  
Sibylle Bremer-Streck ◽  
Shruthi Ramachandra ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Aromatic Amino Acid ◽  
Candida Glabrata ◽  
Genomic Structure ◽  
Aromatic Amino Acids ◽  
Sole Source ◽  
Upstream Region ◽  
Content Type ◽  
Aromatic Amino Acid Aminotransferase

ABSTRACTThe ability to acquire nutrients during infections is an important attribute in microbial pathogenesis. Amino acids are a valuable source of nitrogen if they can be degraded by the infecting organism. In this work, we analyzed histidine utilization in the fungal pathogen of humansCandida glabrata. Hemiascomycete fungi, likeC. glabrataorSaccharomyces cerevisiae, possess no gene coding for a histidine ammonia-lyase, which catalyzes the first step of a major histidine degradation pathway in most other organisms. We show thatC. glabratainstead initializes histidine degradation via the aromatic amino acid aminotransferase Aro8. AlthoughARO8is also present inS. cerevisiaeand is induced by extracellular histidine, the yeast cannot use histidine as its sole nitrogen source, possibly due to growth inhibition by a downstream degradation product. Furthermore,C. glabratarelies only on Aro8 for phenylalanine and tryptophan utilization, sinceARO8, but not its homologueARO9, was transcriptionally activated in the presence of these amino acids. Accordingly, anARO9deletion had no effect on growth with aromatic amino acids. In contrast, inS. cerevisiae,ARO9is strongly induced by tryptophan and is known to support growth on aromatic amino acids. Differences in the genomic structure of theARO9gene betweenC. glabrataandS. cerevisiaeindicate a possible disruption in the regulatory upstream region. Thus, we show that, in contrast toS. cerevisiae,C. glabratahas adapted to use histidine as a sole source of nitrogen and that the aromatic amino acid aminotransferase Aro8, but not Aro9, is the enzyme required for this process.

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