Study on Active Site, PQQ, of Fungal Amine Oxidase

1991 ◽  
pp. 495-497
Author(s):  
H. KAMAGAI ◽  
Y. SHIMADA ◽  
H. TSUCHIYAMA ◽  
T. TOCHIKURA ◽  
H. YAMADA ◽  
...  
Keyword(s):  
Active Site ◽  
Amine Oxidase

Active site residue involvement in monoamine or diamine oxidation catalysed by pea seedling amine oxidase

FEBS Journal ◽  
2011 ◽  
Vol 278 (8) ◽  
pp. 1232-1243 ◽  
Author(s):  
Maria Luisa Di Paolo ◽  
Michele Lunelli ◽  
Monika Fuxreiter ◽  
Adelio Rigo ◽  
Istvan Simon ◽  
...  
Keyword(s):  
Active Site ◽  
Amine Oxidase ◽  
Active Site Residue ◽  
Pea Seedling

N-alkanamines as substrates to probe the hydrophobic region of bovine serum amine oxidase active site: A kinetic and spectroscopic study

2007 ◽  
Vol 465 (1) ◽  
pp. 50-60 ◽  
Author(s):  
Maria Luisa Di Paolo ◽  
Carmine Pesce ◽  
Michele Lunelli ◽  
Marina Scarpa ◽  
Adelio Rigo
Keyword(s):  
Spectroscopic Study ◽  
Active Site ◽  
Bovine Serum ◽  
Amine Oxidase ◽  
Hydrophobic Region

Purification and active-site characterization of equine plasma amine oxidase

1994 ◽  
Vol 56 (2) ◽  
pp. 127-141 ◽  
Author(s):  
Scott R. Carter ◽  
Michele A. McGuirl ◽  
Doreen E. Brown ◽  
David M. Dooley
Keyword(s):  
Active Site ◽  
Amine Oxidase ◽  
Site Characterization ◽  
Equine Plasma ◽  
Plasma Amine Oxidase

scholarly journals Unique protonation states of aspartate and topaquinone in the active site of copper amine oxidase

RSC Advances ◽  
2020 ◽  
Vol 10 (63) ◽  
pp. 38631-38639
Author(s):  
Mitsuo Shoji ◽  
Takeshi Murakawa ◽  
Mauro Boero ◽  
Yasuteru Shigeta ◽  
Hideyuki Hayashi ◽  
...  
Keyword(s):  
Biogenic Amines ◽  
Active Site ◽  
Amine Oxidase ◽  
First Principle ◽  
Amine Oxidases ◽  
Oxidative Deamination ◽  
Copper Amine Oxidase ◽  
First Principle Calculations ◽  
Copper Amine Oxidases ◽  
Copper Amine

Copper amine oxidases catalyze the oxidative deamination of biogenic amines. We investigated the unique protonation states in the active site using first-principle calculations.

An Unexpected Role for the Active Site Base in Cofactor Orientation and Flexibility in the Copper Amine Oxidase fromHansenula polymorpha†

Biochemistry ◽  
1999 ◽  
Vol 38 (26) ◽  
pp. 8204-8216 ◽  
Author(s):  
Julie Plastino ◽  
Edward L. Green ◽  
Joann Sanders-Loehr ◽  
Judith P. Klinman
Keyword(s):  
Active Site ◽  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
Copper Amine

scholarly journals Probing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue

2002 ◽  
Vol 365 (3) ◽  
pp. 809-816 ◽  
Author(s):  
Colin G. SAYSELL ◽  
Winston S. TAMBYRAJAH ◽  
Jeremy M. MURRAY ◽  
Carrie M. WILMOT ◽  
Simon E.V. PHILLIPS ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Active Site ◽  
Amine Oxidase ◽  
Reaction Pathway ◽  
Strong Support ◽  
Reversible Inhibitor ◽  
Wild Type ◽  
Wild Type Enzyme ◽  
Binding Data ◽  
Copper Amine

Copper amine oxidases are homodimeric enzymes containing one Cu2+ ion and one 2,4,5-trihydroxyphenylalanine quinone (TPQ) per monomer. Previous studies with the copper amine oxidase from Escherichia coli (ECAO) have elucidated the structure of the active site and established the importance in catalysis of an active-site base, Asp-383. To explore the early interactions of substrate with enzyme, we have used tranylcypromine (TCP), a fully reversible competitive inhibitor, with wild-type ECAO and with the active-site base variants D383E and D383N. The formation of an adduct, analogous to the substrate Schiff base, between TCP and the TPQ cofactor in the active site of wild-type ECAO and in the D383E and D383N variants has been investigated over the pH range 5.5–9.4. For the wild-type enzyme, the plot of the binding constant for adduct formation (Kb) against pH is bell-shaped, indicating two pKas of 5.8 and ∼8, consistent with the preferred reaction partners being the unprotonated active-site base and the protonated TCP. For the D383N variant, the reaction pathway involving unprotonated base and protonated TCP cannot occur, and binding must follow a less favoured pathway with unprotonated TCP as reactant. Surprisingly, for the D383E variant, the Kb versus pH behaviour is qualitatively similar to that of D383N, supporting a reaction pathway involving unprotonated TCP. The TCP binding data are consistent with substrate binding data for the wild type and the D383E variant using steady-state kinetics. The results provide strong support for a protonated amine being the preferred substrate for the wild-type enzyme, and emphasize the importance of the active-site base, Asp-383, in the primary binding event.

scholarly journals Reconstitution of Cu2+-depleted bovine serum amine oxidase with Co2+*

1998 ◽  
Vol 330 (1) ◽  
pp. 383-387 ◽  
Author(s):  
Enzo AGOSTINELLI ◽  
Giovanna DE MATTEIS ◽  
Bruno MONDOVÌ ◽  
Laura MORPURGO
Keyword(s):  
Active Site ◽  
Bovine Serum ◽  
Oxidase Activity ◽  
Amine Oxidase ◽  
Semiquinone Radical ◽  
Copper Site ◽  
Benzylamine Oxidase ◽  
Topa Quinone ◽  
Derivatives Of ◽  
Active Subunits

Two different Cu2+-depleted derivatives of bovine serum amine oxidase (BSAO) have recently been prepared, which contain about 0.5 mol/dimer of phenylhydrazine-reactive topa quinone (TPQ) cofactor and, depending on the reagents used, about 0.2 or 0.7 residual Cu2+/dimer [Agostinelli, De Matteis, Sinibaldi, Mondovì and Morpurgo (1997) Biochem. J. 324, 497-501]. The benzylamine oxidase activity of both derivatives was < 5% and increased up to ≈ 20% on incorporation of Co2+, irrespective of the residual Cu2+ content, which was unaffected by the treatment according to atomic absorption and ESR spectroscopy. The residual Cu2+ ions appeared to be distributed one per dimer and to be bound to inactive subunits, whereas Co2+ was bound to active subunits. The change in the active site had an appreciable influence on the kinetic behaviour. With several amines, the kinetic parameters, Km and kc, measured for Co2+-BSAO were different from those for native BSAO. This excludes the possibility that the catalytic activity was due to residual Cu2+. Furthermore, Co2+ restored to nearly native level the intensity of the TPQ 480 nm band and the reactions with phenylhydrazine or benzylhydrazine, which had been slowed down or abolished, respectively, in Cu2+-depleted samples. The CD spectrum, measured for the derivative with low Cu2+ content, was compatible with Co2+ binding to the copper site. The amine oxidase activity of the Co2+ derivative, which cannot form a semiquinone radical as an intermediate of the catalytic reaction, strongly suggests that the Cu+-semiquinone is not an obligatory intermediate of BSAO catalytic pathway.

Sign in / Sign up

Export Citation Format

Share Document