Phylogenetic and biochemical characterization of a novel cluster of intracellular fungal α-amylase enzymes
| Autor: | Kaaij, R.M. van der, Janeček, Š., Maarel, M.J.E.C. van der, Dijkhuizen, L. |
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| Přispěvatelé: | TNO Kwaliteit van Leven |
| Jazyk: | angličtina |
| Rok vydání: | 2007 |
| Předmět: |
Basidiomycetes
amylase gene overexpression Histoplasma Molecular Sequence Data gene sequence phylogeny gene cluster Food technology Substrate Specificity Fungal Proteins alpha-Amylase Ascomycota Cell Wall protein purification Animals Amino Acid Sequence Glucans enzyme analysis Nutrition nonhuman amylase D Ajellomyces capsulatus starch Basidiomycota article Fungi nucleotide sequence glucan sequence homology Ascomycetes maltotriose enzyme activity Histoplasma capsulatum priority journal Aspergillus niger Sequence Alignment amylase 1p |
| Zdroj: | Microbiology, 12, 153, 4003-4015 |
| Popis: | Currently known fungal α-amylases are well-characterized extracellular enzymes that are classified into glycoside hydrolase subfamily GH13_1. This study describes the identification, and phylogenetic and biochemical analysis of novel intracellular fungal α-amylases. The phylogenetic analysis shows that they cluster in the recently identified subfamily GH135_5 and display very low similarity to fungal α-amylases of family GH13_1. Homologues of these intracellular enzymes are present in the genome sequences of all filamentous fungi studied, including ascomycetes and basidiomycetes. One of the enzymes belonging to this new group, Amy1p from Histoplasma capsulatum, has recently been functionally linked to the formation of cell wall α-glucan. To study the biochemical characteristics of this novel cluster of α-amylases, we overexpressed and purified a homologue from Aspergillus niger, AmyD, and studied its activity product profile with starch and related substrates. AmyD has a relatively low hydrolysing activity on starch (2.2 U mg-1), producing mainly maltotriose. A possible function of these enzymes in relation to cell wall α-glucan synthesis is discussed. © 2007 SGM. |
| Databáze: | OpenAIRE |
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