Browsing by Author "Peirano, Alessandra"

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    Characterization of crystals of Penicillium purpurogenum acetyl xylan esterase from high-resolution X-ray diffraction
    (1996) Pangborn, Walter; Erman, Mary; Li, Naiyin; Burkhart, Brian M.; Pletnev, Vladimir Z.; Duax, William L.; Gutiérrez Ilabaca, Rodrigo Antonio; Peirano, Alessandra; Eyzaguirre, Jaime; Thiel, Daniel J.; Ghosh, Debashis
    Acetyl xylan esterase from Penicillium purpurogenum, a single-chain 23 kDa member of a newly characterized family of esterases that cleaves side chain ester linkages in xylan, has been crystallized. The crystals diffract to better than 1 Å resolution at the Cornell High Energy Synchrotron Source (CHESS) and are highly stable in the synchrotron radiation. The space group is P212121 and cell dimensions are a = 34.9 Å, b = 61.0 Å, c = 72.5 Å.
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    Penicillium purpurogenum produces a family 1 acetyl xylan esterase containing a carbohydrate-binding module
    (2006) Gordillo, Felipe; Caputo, Valentina; Peirano, Alessandra; Chavez, Renato; Van Beeumen, Jozef; Vandenberghe, Isabel; Claeyssens, Marc; Bull, Paulina; Ravanal, Maria Cristina; Eyzaguirre, Jaime
    At least three acetyl xylan esterases (AXE I, II and III) are secreted by Penicillium purpurogenum. This publication describes more detailed work on AXE I and its gene. AXE I binds cellulose but not xylan; it is glycosylated and inactivated by phenylmethylsulphonyl fluoride, showing that it is a serine esterase. The axe1 gene presents an open reading frame of 1278 bp, including two introns of 68 and 61 bp; it codes for a signal peptide of 31 residues and a mature protein of 351 amino acids (molecular weight 36,693). AXE I has a modular structure: a catalytic module at the amino terminus belonging to family I of the carbohydrate esterases, a linker rich in serines and threonines, and a family 1 carboxy terminal carbohydrate binding module (CBM). The CBM is similar to that of AXE from Trichoderma reesei, (with a family 5 catalytic module) indicating that the genes for catalytic modules and CBMs have evolved separately, and that they have been linked by gene fusion. The promoter sequence of axe1 contains several putative sequences for binding of gene expression regulators also found in other family 1 esterase gene promoters. It is proposed that AXE I and II act in succession in xylan degradation; first, xylan is attacked by AXE I and other xylanases possessing CBMs (which facilitate binding to lignocellulose), followed by other enzymes acting mainly on soluble substrates. (c) 2006 The British Mycological Society. Published by Elsevier Ltd. All rights reserved.