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Titolo:
Structural and kinetic characterization of native laccases from Pleurotas ostreatus, Rigidoporus lignosus, and Trametes trogii
Autore:
Garzillo, AM; Colao, MC; Buonocore, V; Oliva, R; Falcigno, L; Saviano, M; Santoro, AM; Zappala, R; Bonomo, RP; Bianco, C; Giardina, P; Palmieri, G; Sannia, G;
Indirizzi:
Univ Naples Federico II, Dipartimento Chim Organ & Biochim, I-80126 Naples, Italy Univ Naples Federico II Naples Italy I-80126 chim, I-80126 Naples, Italy Univ Tuscia, Dipartimento Agrobiol & Agrochim, I-01100 Viterbo, Italy UnivTuscia Viterbo Italy I-01100 iol & Agrochim, I-01100 Viterbo, Italy Univ Naples Federico II, Dipartimento Chim, I-80126 Naples, Italy Univ Naples Federico II Naples Italy I-80126 Chim, I-80126 Naples, Italy Ctr Studio Biocristallog CNR, I-80134 Naples, Italy Ctr Studio Biocristallog CNR Naples Italy I-80134 I-80134 Naples, Italy Univ Catania, Dipartimento Sci Chim, I-95125 Catania, Italy Univ Catania Catania Italy I-95125 ento Sci Chim, I-95125 Catania, Italy
Titolo Testata:
JOURNAL OF PROTEIN CHEMISTRY
fascicolo: 3, volume: 20, anno: 2001,
pagine: 191 - 201
SICI:
0277-8033(200104)20:3<191:SAKCON>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
ASCORBATE OXIDASE; CRYSTAL-STRUCTURE; FUNGAL LACCASES; PH; RESOLUTION; STABILITY; PROTEINS; PROFILE; GENE;
Keywords:
laccase; Pleurotus ostreatus; Rigidoporus lignosus; Trametes trogii; redox potential;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
27
Recensione:
Indirizzi per estratti:
Indirizzo: Sannia, G Univ Naples Federico II, Dipartimento Chim Organ & Biochim, Complesso UnivMonte S Angelo, I-80126 Naples, Italy Univ Naples Federico II Complesso Univ Monte S Angelo Naples Italy I-80126
Citazione:
A.M. Garzillo et al., "Structural and kinetic characterization of native laccases from Pleurotas ostreatus, Rigidoporus lignosus, and Trametes trogii", J PROTEIN C, 20(3), 2001, pp. 191-201

Abstract

A comparative study has been performed on five native laccases purified from the three basidiomycete fungi Pleurotus ostreatus, Rigidoporus lignosus,and Trametes trogii to relate their different catalytic capacities to their structural properties. Spectroscopic absorption features and EPR spectra at various pH values of the five enzymes are very similar and typical of the blue oxidases. The analysis of the dependence of kinetic parameters on pHsuggested that a histidine residue is involved in the binding of nonphenolic substrates, whereas both a histidine and an acidic residue may be involved in the binding of phenolic compounds. His and an Asp residue are indeed found at the bottom of a cavity which may be regarded as a suitable substrate channel for approaching to type I copper in the 3D homology models of the two laccases from Pleuorotus ostreatus (POXC and POXA1b) whose sequences are known.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/10/20 alle ore 21:26:00