BENZALDEHYDE LYASE, A NOVEL THIAMINE PPI-REQUIRING ENZYME, FROM PSEUDOMONAS-FLUORESCENS BIOVAR-I

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dc.contributor.authorGONZALEZ, B
dc.contributor.authorVICUNA, R
dc.date.accessioned2025-01-23T19:23:59Z
dc.date.available2025-01-23T19:23:59Z
dc.date.issued1989
dc.description.abstractPseudomonas fluorescens biovar I can grow on benzoin as the sole carbon and energy source. This ability is due to benzaldehyde lyase, a new type of enzyme that irreversibly cleaves the acyloin linkage of benzoin, producing two molecules of benzaldehyde. Benzaldehyde lyase was purified 70-fold and found to require catalytic amounts of thiamine PPi (TPP) and a divalent cation as cofactors. Optimal activity was obtained with a 1.0 mM concentration of Mn2+, Mg2+, or Ca2+. Gel permeation chromatography indicated a native molecular weight of 80,000, whereas the enzyme migrated in sodium dodecyl sulfate-containing polyacrylamide gels as a single polypeptide with a molecular weight of 53,000. Benzaldehyde lyase is highly specific; of a variety of structurally related compounds tested, only benzoin and benzoin and anisoin (4,4''-dimethoxybenzoin) acted as substrates, their apparent Kms being 9.0 .times. 10-3 and 3.25 .times. 10-2 mM, respectively. A catalytic mechanism for the enzyme is proposed.
dc.fuente.origenWOS
dc.identifier.eissn1098-5530
dc.identifier.issn0021-9193
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/99293
dc.identifier.wosidWOS:A1989U427300018
dc.issue.numero5
dc.language.isoen
dc.pagina.final2405
dc.pagina.inicio2401
dc.revistaJournal of bacteriology
dc.rightsacceso restringido
dc.titleBENZALDEHYDE LYASE, A NOVEL THIAMINE PPI-REQUIRING ENZYME, FROM PSEUDOMONAS-FLUORESCENS BIOVAR-I
dc.typeartículo
dc.volumen171
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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