Molecular characterization of a Penicillium chrysogenum exo-1,5-alpha-L-arabinanase that is structurally distinct from other arabinan-degrading enzymes.
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 alpha-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.
Sakamoto
Tatsuji
T
Division of Applied Biochemistry, Graduate School of Agriculture and Biological Sciences, Osaka Prefecture University, Osaka 599-8531, Japan. sakamoto@biochem.osakafu-u.ac.jp
Ihara
Hideshi
H
Shibano
Asako
A
Kasai
Naoya
N
Inui
Hiroshi
H
Kawasaki
Haruhiko
H
D000595:Amino Acid Sequence; D001089:Arabinose / Q000378:metabolism; D001483:Base Sequence; D002384:Catalysis; D004926:Escherichia coli / Q000235:genetics; D005800:Genes, Fungal; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000145:classification / Q000302:isolation & purification; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008969:Molecular Sequence Data; D010408:Penicillium chrysogenum / Q000201:enzymology*; D017433:Protein Structure, Secondary; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D013696:Temperature
D011993:Recombinant Fusion Proteins; D001089:Arabinose; D006026:Glycoside Hydrolases; C434938:exo-alpha-L-arabinanase