TY - JOUR
T1 - Purification and characterization of peroxisomal L-pipecolic acid oxidase from monkey liver
AU - Mihalik, Stephanie J.
AU - McGuinness, Martina
AU - Watkins, Paul A.
N1 - Copyright:
Copyright 2007 Elsevier B.V., All rights reserved.
PY - 1991/3/15
Y1 - 1991/3/15
N2 - L-Pipecolic acid oxidase has been purified to near homogeneity from Rhesus monkey liver. The protein, a yellow monomer, has a molecular weight of 46,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and a pI of 8.9. It contains a covalently bound flavin with absorption maxima at 457 and 383 nm and a shoulder at 480 nm. The purified enzyme is most reactive toward L-pipecolic acid, with lesser reactivities toward L-proline and sarcosine. The enzyme has no significant reactivity toward the D-enantiomer of pipecolic acid or toward any other amino acid tested. Benzoic acid is a competitive inhibitor of the enzyme with a Ki of 750 μM. The Km of the purified enzyme is 3.7 mM for L-pipecolic acid. With less purified preparations, the reaction product is α-aminoadipic acid. The purified enzyme, however, produces an intermediate which reacts with ortho-aminobenzaldehyde to form an α-aminoadipic acid semialdehyde adduct. Thus, the formation of α-aminoadipic acid requires at least two enzymes.
AB - L-Pipecolic acid oxidase has been purified to near homogeneity from Rhesus monkey liver. The protein, a yellow monomer, has a molecular weight of 46,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and a pI of 8.9. It contains a covalently bound flavin with absorption maxima at 457 and 383 nm and a shoulder at 480 nm. The purified enzyme is most reactive toward L-pipecolic acid, with lesser reactivities toward L-proline and sarcosine. The enzyme has no significant reactivity toward the D-enantiomer of pipecolic acid or toward any other amino acid tested. Benzoic acid is a competitive inhibitor of the enzyme with a Ki of 750 μM. The Km of the purified enzyme is 3.7 mM for L-pipecolic acid. With less purified preparations, the reaction product is α-aminoadipic acid. The purified enzyme, however, produces an intermediate which reacts with ortho-aminobenzaldehyde to form an α-aminoadipic acid semialdehyde adduct. Thus, the formation of α-aminoadipic acid requires at least two enzymes.
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M3 - Article
C2 - 2002029
AN - SCOPUS:0025805681
SN - 0021-9258
VL - 266
SP - 4822
EP - 4830
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 8
ER -