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Molecular characterization of a Penicillium chrysogenum exo‐1,5‐α‐ L ‐arabinanase that is structurally distinct from other arabinan‐degrading enzymes
Author(s) -
Sakamoto Tatsuji,
Ihara Hideshi,
Shibano Asako,
Kasai Naoya,
Inui Hiroshi,
Kawasaki Haruhiko
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(04)00106-1
Subject(s) - penicillium chrysogenum , neurospora crassa , biochemistry , complementary dna , biology , escherichia coli , peptide sequence , enzyme , gene , recombinant dna , nucleic acid sequence , mutant
The nucleotide sequence of the abnx cDNA gene, which encodes an exo‐arabinanase (Abnx) of Penicillium chrysogenum 31B, was determined. Abnx was found to be structurally distinct from known arabinan‐degrading enzymes based on its amino acid sequence and a hydrophobic cluster analysis. The protein in the protein database with the highest similarity to Abnx was the Neurospora crassa conserved hypothetical protein. The abnx cDNA gene product expressed in Escherichia coli catalyzed the release of arabinobiose from α‐1,5‐ L ‐arabinan. The activity of the recombinant Abnx towards a series of arabino‐oligosaccharides, as expressed by k cat / K m value, was greatest with arabinohexaose.