Abstract:
:Pseudomonas L-phenylalanine oxidase (deaminating and decarboxylating) mainly catalyzes oxygenation when L-phenylalanine is used as the substrate, but oxidation when L-methionine is used as the substrate. Using [C(alpha)-H]-DL-methionine and [C(alpha)-D]-DL-methionine as substrate, the reductive half reaction of FAD cofactor of enzyme has been studied by stopped-flow spectrophotometry. The rate of reduction of FAD cofactor has a kinetic isotope effect (KIE) of 5.4 and 4.1 in the absence and presence of 30% glycerol, respectively. The KIE is independent of temperature, but the rates of the reductive half reaction are dependent on temperature, indicating that thermally induced motion at the active site drives the H-transfer reaction by H-tunneling.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Ohta Y,Mukouyama EB,Suzuki Hdoi
10.1093/jb/mvj049keywords:
subject
Has Abstractpub_date
2006-03-01 00:00:00pages
551-5issue
3eissn
0021-924Xissn
1756-2651pii
139/3/551journal_volume
139pub_type
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