TY - JOUR
T1 - Purification, cloning, and three-dimensional structure prediction of Micrococcus luteus FAD-containing tyramine oxidase
AU - Roh, Jung Hyeob
AU - Wouters, Johan
AU - Depiereux, Eric
AU - Yukawa, Hideaki
AU - Inui, Masayuki
AU - Minami, Hiromichi
AU - Suzuki, Hideyuki
AU - Kumagai, Hidehiko
PY - 2000/2/16
Y1 - 2000/2/16
N2 - The FAD-containing tyramine oxidase enzyme and gene from the Gram (+) bacterium Micrococcus luteus were isolated, and computer prediction was used to propose a preliminary 3D model of the protein. A 2.8-kb Sau3AI fragment containing the structural gene of tyramine oxidase was cloned from a M. luteus genomic DNA library. The 1332 bp gene encodes a protein of 443 amino acids, with a calculated molecular mass of 49.1 kDa. The enzyme was found to be a homodimer with a molecular weight of 49,000. It oxidizes tyramine, adrenaline, 3-hydroxytyramine, dopamine, and noradrenaline, and was reversibly inhibited by FAD-containing monoamine oxidase A and B specific inhibitors. Sequence comparison show that tyramine oxidase is smaller than other FAD-amine oxidases but that it contains well-conserved amino acid residues reported in all other FAD-amine oxidases. A hypothetical three-dimensional structure of tyramine oxidase has also been proposed based on secondary structure predictions, threading, and comparative modeling. (C) 2000 Academic Press.
AB - The FAD-containing tyramine oxidase enzyme and gene from the Gram (+) bacterium Micrococcus luteus were isolated, and computer prediction was used to propose a preliminary 3D model of the protein. A 2.8-kb Sau3AI fragment containing the structural gene of tyramine oxidase was cloned from a M. luteus genomic DNA library. The 1332 bp gene encodes a protein of 443 amino acids, with a calculated molecular mass of 49.1 kDa. The enzyme was found to be a homodimer with a molecular weight of 49,000. It oxidizes tyramine, adrenaline, 3-hydroxytyramine, dopamine, and noradrenaline, and was reversibly inhibited by FAD-containing monoamine oxidase A and B specific inhibitors. Sequence comparison show that tyramine oxidase is smaller than other FAD-amine oxidases but that it contains well-conserved amino acid residues reported in all other FAD-amine oxidases. A hypothetical three-dimensional structure of tyramine oxidase has also been proposed based on secondary structure predictions, threading, and comparative modeling. (C) 2000 Academic Press.
UR - http://www.scopus.com/inward/record.url?scp=0034673370&partnerID=8YFLogxK
U2 - 10.1006/bbrc.2000.2113
DO - 10.1006/bbrc.2000.2113
M3 - Article
C2 - 10679196
AN - SCOPUS:0034673370
SN - 0006-291X
VL - 268
SP - 293
EP - 297
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -