| Autor: |
A E, Kuhm, H J, Knackmuss, A, Stolz |
| Rok vydání: |
1993 |
| Předmět: |
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| Zdroj: |
The Journal of biological chemistry. 268(13) |
| ISSN: |
0021-9258 |
| Popis: |
2'-Hydroxybenzalpyruvate aldolase catalyzes the cleavage of 2'-hydroxybenzalpyruvate to salicylaldehyde and pyruvate. This reaction is part of the degradative pathways for naphthalene and naphthalenesulfonates by bacteria. 2'-Hydroxybenzalpyruvate aldolase has been purified to homogeneity from a bacterium that degrades naphthalenesulfonates (strain BN6). The enzyme has a molecular weight of about 120,000 and is composed of identical subunits with a molecular weight of about 38,500. Thus the enzyme appears to exist as a trimeric oligomer. The NH2-terminal amino acid sequence did not show significant homology to other published amino acid sequences. Extensive loss of enzyme activity occurred when the enzyme was incubated with 2'-hydroxybenzalpyruvate in the presence of sodium borhydride. This suggested the intermediate formation of a stable Schiff base between enzyme and substrate. 2'-Hydroxybenzalpyruvate aldolase was inhibited by p-chloromercuribenzoate and by the reaction product salicylaldehyde. The enzyme converted 2'-hydroxybenzalpyruvate, 2',4'- and 2',6'-dihydroxybenzalpyruvate. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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