An eleven amino acid residue deletion expands the substrate specificity of acetyl xylan esterase II (AXE II) from <i>Penicillium purpurogenum</i>

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dc.contributor.authorColombres, Marcela
dc.contributor.authorGarate, Jose A.
dc.contributor.authorLagos, Carlos F.
dc.contributor.authorAraya-Secchi, Raul
dc.contributor.authorNorambuena, Patricia
dc.contributor.authorQuiroz, Soledad
dc.contributor.authorLarrondo, Luis
dc.contributor.authorPerez-Acle, Tomas
dc.contributor.authorEyzaguirre, Jaime
dc.date.accessioned2025-01-21T01:05:13Z
dc.date.available2025-01-21T01:05:13Z
dc.date.issued2008
dc.description.abstractThe soft-rot fungus Penicillium purpurogenum secretes to the culture medium a variety of enzymes related to xylan biodegradation, among them three acetyl xylan esterases (AXE I, II and III). AXE II has 207 amino acids; it belongs to family 5 of the carbohydrate esterases and its structure has been determined by X-ray crystallography at 0.9 angstrom resolution (PDB 1G66). The enzyme possesses the alpha/beta hydrolase fold and the catalytic triad typical of serine esterases (Ser90, His187 and Asp175). AXE II can hydrolyze esters of a large variety of alcohols, but it is restricted to short chain fatty acids. An analysis of its three-dimensional structure shows that a loop that covers the active site may be responsible for this strict specificity. Cutinase, an enzyme that hydrolyzes esters of long chain fatty acids and shows a structure similar to AXE II, lacks this loop. In order to generate an AXE II with this broader specificity, the preparation of a mutant lacking residues involving this loop (Gly104 to Ala114) was proposed. A set of molecular simulation experiments based on a comparative model of the mutant enzyme predicted a stable structure. Using site-directed mutagenesis, the loop's residues have been eliminated from the AXE II cDNA. The mutant protein has been expressed in Aspergillus nidulans A722 and Pichia pastoris, and it is active towards a range of fatty acid esters of up to at least 14 carbons. The availability of an esterase with broader specificity may have biotechnological applications for the synthesis of sugar esters.
dc.fuente.origenWOS
dc.identifier.doi10.1007/s10822-007-9149-4
dc.identifier.eissn1573-4951
dc.identifier.issn0920-654X
dc.identifier.urihttps://doi.org/10.1007/s10822-007-9149-4
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/95859
dc.identifier.wosidWOS:000252540900002
dc.issue.numero1
dc.language.isoen
dc.pagina.final28
dc.pagina.inicio19
dc.revistaJournal of computer-aided molecular design
dc.rightsacceso restringido
dc.subjectacetyl xylan esterase
dc.subjectcutinase
dc.subjectcomparative modeling
dc.subjectmutagenesis
dc.subjectPenicillium purpurogenum
dc.subject.ods07 Affordable and Clean Energy
dc.subject.ods12 Responsible Consumption and Production
dc.subject.odspa07 Energía asequible y no contaminante
dc.subject.odspa12 Producción y consumo responsable
dc.titleAn eleven amino acid residue deletion expands the substrate specificity of acetyl xylan esterase II (AXE II) from <i>Penicillium purpurogenum</i>
dc.typeartículo
dc.volumen22
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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