pH and kinetic isotope effects on the reductive half-reaction of D-amino acid oxidase

Biochemistry ◽  
1992 ◽  
Vol 31 (35) ◽  
pp. 8207-8215 ◽  
Author(s):  
John M. Denu ◽  
Paul F. Fitzpatrick
2001 ◽  
Vol 268 (21) ◽  
pp. 5504-5520 ◽  
Author(s):  
Christopher M. Harris ◽  
Loredano Pollegioni ◽  
Sandro Ghisla

FEBS Letters ◽  
1970 ◽  
Vol 6 (1) ◽  
pp. 22-24 ◽  
Author(s):  
Kunio Yagi ◽  
Morimitsu Nishikimi ◽  
Nobuko Ohishi ◽  
Akiko Takai

2000 ◽  
Vol 122 (51) ◽  
pp. 12896-12897 ◽  
Author(s):  
Kevin A. Kurtz ◽  
Mark A. Rishavy ◽  
W. W. Cleland ◽  
Paul F. Fitzpatrick

2020 ◽  
Vol 168 (5) ◽  
pp. 509-514
Author(s):  
Małgorzata Pająk

Abstract l-Amino acid oxidase (LAAO) is widely distributed in nature and shows important biological activity. It induces cell apoptosis and has antibacterial properties. This study was designed to investigate the effect of methyl substituent on its activity as methylated derivatives of l-tyrosine, labelled with short-lived B+ emitters, have been used in oncological diagnostics. To study isotope effects in the oxidative deamination of O-methyl-l-tyrosine, the deuterated isotopomer, i.e. O-methyl-[2-2H]-l-tyrosine, was synthesized by isotope exchange, catalyzed enzymatically by tryptophanase. Isotope effects were determined using the spectrophotometric non-competitive method. The values of isotope effects indicate that the α-C–H bond cleavage occurs in the rate determining step of the investigated reaction and α-hydrogen plays a role in the substrate binding process at the enzyme active site. The inhibitory effect on LAAO activity was studied with α-methyl-l-tyrosine and N-methyl-l-tyrosine. The mode of inhibition was determined based on Lineweavear–Burk plots intersections. α-Methyl-l-tyrosine has been found a mixed type inhibitor of the investigated enzyme, whereas N-methyl-l-tyrosine is a non-competitive inhibitor of LAAO.


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