JBC, Vol. 252, Issue 8, 2648-2656, Apr, 1977
Crystalline hemoprotein from Pseudomonas that catalyzes oxidation of side chain of tryptophan and other indole derivatives
K. Takai, H. Ushiro, Y. Noda, S. Narumiya and T. Tokuyama
A new enzyme which catalyzes the oxidation of the side chain of tryptophan
and other indole derivatives, has been purified to apparent homogeneity
from Pseudomonas and crystallized. The overall purification was about
25-fold with a yield of 4.5%. The purified enzyme was apparently
homogeneous as judged by polyacrylamide gel electrophoresis. The molecular
weight estimated by gel filtration was approximately 280,000 and
sedimentation coefficient (S20,w) was 11 by sucrose density gradient
ultracentrifugation. The absorption spectra indicated that the enzyme was a
hemoprotein. The purified enzyme was shown to catalyze the reaction in
which 1 mol each of NH3 and CO2 was formed at the expense of 1 mol each of
L-tryptophan and molecular oxygen. Neither peroxidase nor catalase activity
was detected in the purified enzyme and no formation of H2O2 was observed
during the enzyme reaction. The product(s) of the reaction was unstable but
was converted to and was identified as its stable quinoxaline derivative,
2-(3-indolyl)quinoxaline, in the presence of o-phenylenediamine. These
results indicate that the product of the reaction was
3-indolylglycoaldehyde or 3-indolylglyoxal. A variety of other indole
derivatives such as D-tryptophan, 5-hydroxyl-L-tryptophan, tryptamine,
serotonin, melatonin, N-acetyl-L-tryptophan, N-acetyl-L-tryptophanamide,
3-indoleacetamide, 3-indolelactic acid, 3-indolepropionic acid,
3-indoleethanol, and skatole were also substrates.
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