Purification and characterization of a novel type of protocatechuate 3,4-dioxygenase with the ability to oxidize 4-sulfocatechol |
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Authors: | Angela Hammer Andreas Stolz H-J Knackmuss |
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Institution: | Institut für Mikrobiologie, Universit?t Stuttgart, Allmandring 31, D-70569 Stuttgart, Germany Tel. +49-711-685-5487; Fax +49-711-685-5725, DE
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Abstract: | 4-Aminobenzenesulfonate is degraded via 4-sulfocatechol by a mixed bacterial culture that consists of Hydrogenophaga palleronii strain S1 and Agrobacterium radiobacter strain S2. From the 4-sulfocatechol-degrading organism A. radiobacter strain S2, a dioxygenase that converted 4-sulfocatechol to 3-sulfomuconate was purified to homogeneity. The purified enzyme
also converted protocatechuate with a similar catalytic activity to 3-carboxy-cis,cis-muconate. Furthermore, the purified enzyme oxidized 3,4-dihydroxyphenylacetate, 3,4-dihydroxycinnamate, catechol, and 3-
and 4-methylcatechol. The enzyme had a mol. wt. of about 97,400 as determined by gel filtration and consisted of two different
types of subunits with mol. wt. of about 23,000 and 28,500. The NH2-terminal amino acid sequences of the two subunits were determined. An isofunctional dioxygenase was partially purified from
H. palleronii strain S1. A. radiobacter strain S2 also induced, after growth with 4-sulfocatechol, an „ordinary“ protocatechuate 3,4-dioxygenase that did not oxidize 4-sulfocatechol.
This enzyme was also purified to homogeneity, and its catalytic and structural characteristics were compared to the „4-sulfocatechol-dioxygenase“
from the same strain.
Received: 5 February 1996 / Accepted: 18 April 1996 |
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Keywords: | 4-Aminobenzenesulfonate 4-Sulfocatechol Xenobiotics Biodegradation Agrobacterium radiobacter Protocatechuate 3 4-dioxygenase Intradiol cleavage |
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