The structure of maize polyamine oxidase K300M mutant in complex with the natural substrates provides a snapshot of the catalytic mechanism of polyamine oxidation. (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• The structure of maize polyamine oxidase K300M mutant in complex with the natural substrates provides a snapshot of the catalytic mechanism of polyamine oxidation. (Articolo in rivista) (literal)

Anno

• 2011-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1111/j.1742-4658.2010.08000.x (literal)

Alternative label

• Fiorillo A, Federico R, Polticelli F, Boffi A, Mazzei F, Di Fusco M, Ilari A, Tavladoraki P. (2011)
  The structure of maize polyamine oxidase K300M mutant in complex with the natural substrates provides a snapshot of the catalytic mechanism of polyamine oxidation.
  in The FEBS journal (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Fiorillo A, Federico R, Polticelli F, Boffi A, Mazzei F, Di Fusco M, Ilari A, Tavladoraki P. (literal)

Rivista

• ?The ?FEBS journal (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• 1. Univ Roma La Sapienza, Dept Biochem Sci, CNR, IBPM, I-00185 Rome, Italy 2. Univ Aquila, Dept Sci & Biomed Technol, I-67100 Laquila, Italy 3. Univ Roma Tre, Dept Biol, Rome, Italy 4. Univ Roma La Sapienza, Dept Chem & Drug Technol, I-00185 Rome, Italy (literal)

Titolo

• The structure of maize polyamine oxidase K300M mutant in complex with the natural substrates provides a snapshot of the catalytic mechanism of polyamine oxidation. (literal)

Abstract

• Polyamine oxidases are FAD-dependent enzymes catalyzing the oxidation of polyamines at the secondary amino groups. Zea mays PAO (ZmPAO) oxidizes the carbon on the endo-side of the N5-nitrogen of spermidine (Spd) and spermine (Spm). The structure of ZmPAO revealed that the active site is formed by a catalytic tunnel in which the N5 atom of FAD lies in close proximity to the K300 side chain, the only active-site residue conserved in all PAOs. A water molecule, (HOH309), is hydrogen-bound to the amino group of K300 and mutation of this residue results in a 1400-fold decrease in the rate of flavin reduction. The structural studies on the catalytically impaired ZmPAO-K300M mutant described here show that substrates are bound in an 'out-of-register' mode and the HOH309 water molecule is absent in the enzyme-substrate complexes. Moreover, K300 mutation brings about a 60 mV decrease in the FAD redox potential and a 30-fold decrease in the FAD reoxidation rate, within a virtually unaltered geometry of the catalytic pocket. Taken together, these results indicate that the HOH309-K300 couple plays a major role in multiple steps of ZmPAO catalytic mechanism, such as correct substrate binding geometry as well as FAD reduction and reoxidation kinetics. (literal)

Prodotto di

• Biologia strutturale e bioinformatica: struttura-funzione, dinamica e riconoscimento in proteine (SV.P14.008.001) (Modulo)
• Institute of molecular biology and pathology (IBPM) (Istituto)

Autore CNR

• ALBERTO BOFFI (Unità di personale esterno)
• ANDREA ILARI (Unità di personale interno)

Incoming links:

Prodotto

• Institute of molecular biology and pathology (IBPM) (Istituto)
• Biologia strutturale e bioinformatica: struttura-funzione, dinamica e riconoscimento in proteine (SV.P14.008.001) (Modulo)

Autore CNR di

• ANDREA ILARI (Unità di personale interno)
• ALBERTO BOFFI (Unità di personale esterno)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• ?The ?FEBS journal (Rivista)