scholarly journals The organic cofactor in plasma amine oxidase: evidence for pyrroloquinoline quinone and against pyridoxal phosphate

1987 ◽  
Vol 241 (2) ◽  
pp. 603-608 ◽  
Author(s):  
P F Knowles ◽  
K B Pandeya ◽  
F X Rius ◽  
C M Spencer ◽  
R S Moog ◽  
...  
Keyword(s):  
Pyridoxal Phosphate ◽  
Amine Oxidase ◽  
Resonance Raman ◽  
Pyrroloquinoline Quinone ◽  
Spectral Studies ◽  
Amine Oxidases ◽  
Plasma Enzymes ◽  
Bovine Plasma ◽  
Plasma Amine Oxidase ◽  
Derivatives Of

Plasma amine oxidases (EC 1.4.3.6) are classified as containing the organic cofactor pyridoxal phosphate. Biochemical and bioassays on the pig plasma amine oxidase fail to reveal the presence of pyridoxal phosphate and 31P n.m.r. evidence is also inconsistent with pyridoxal phosphate in the enzyme. Resonance Raman spectral studies on phenylhydrazone derivatives of the pig and bovine plasma enzymes have been carried out and comparisons made with the corresponding derivatives of pyridoxal phosphate and pyrroloquinoline quinone (PQQ). The resonance Raman evidence indicates that the cofactor in both plasma amine oxidases is PQQ or a closely related species and not pyridoxal phosphate. The results substantiate earlier reports concerning the identity of the organic cofactor.

scholarly journals Studies on the active site of pig plasma amine oxidase

1989 ◽  
Vol 264 (3) ◽  
pp. 663-669 ◽  
Author(s):  
D Collison ◽  
P F Knowles ◽  
F E Mabbs ◽  
F X Rius ◽  
I Singh ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Active Site ◽  
Oxidase Activity ◽  
Amine Oxidase ◽  
Spectral Characteristics ◽  
Pyrroloquinoline Quinone ◽  
Amine Oxidases ◽  
Assay Procedure ◽  
Plasma Amine Oxidase ◽  
Amine Oxidase Activity

Amine oxidase from pig plasma (PPAO) has two bound Cu2+ ions and at least one pyrroloquinoline quinone (PQQ) moiety as cofactors. It is shown that recovery of activity by copper-depleted PPAO is linear with respect to added Cu2+ ions. Recovery of e.s.r. and optical spectral characteristics of active-site copper parallel the recovery of catalytic activity. These results are consistent with both Cu2+ ions contributing to catalysis. Further e.s.r. studies indicate that the two copper sites in PPAO, unlike those in amine oxidases from other sources, are chemically distinct. These comparative studies establish that non-identity of the Cu2+ ions in PPAO is not a requirement for amine oxidase activity. It is shown through the use of a new assay procedure that there are two molecules of PQQ bound per molecule of protein in PPAO; only the more reactive of these PQQ moieties is required for activity.

Copper x-ray absorption spectroscopic studies of the bovine plasma amine oxidase-sulfide complex

1988 ◽  
Vol 27 (21) ◽  
pp. 3859-3861 ◽  
Author(s):  
Robert A. Scott ◽  
Cheryl E. Cote ◽  
David M. Dooley
Keyword(s):  
Amine Oxidase ◽  
Spectroscopic Studies ◽  
X Ray ◽  
Bovine Plasma ◽  
Plasma Amine Oxidase ◽  
X Ray Absorption

The essential histidine residues of bovine plasma amine oxidase

1975 ◽  
Vol 400 (2) ◽  
pp. 451-460 ◽  
Author(s):  
Shigeko Tsurushiin ◽  
Akira Hiramatsu ◽  
Melvin Inamasu ◽  
Kerry T. Yasunobu
Keyword(s):  
Amine Oxidase ◽  
Histidine Residues ◽  
Bovine Plasma ◽  
Plasma Amine Oxidase
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