Ontology highlight
ABSTRACT:
SUBMITTER: Iwabuchi T
PROVIDER: S-EPMC106976 | biostudies-literature | 1998 Feb
REPOSITORIES: biostudies-literature
Journal of bacteriology 19980201 4
trans-2'-Carboxybenzalpyruvate hydratase-aldolase was purified from a phenanthrene-degrading bacterium, Nocardioides sp. strain KP7, and characterized. The purified enzyme was found to have molecular masses of 38 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 113 kDa by gel filtration chromatography. Thus, the homotrimer of the 38-kDa subunit constituted an active enzyme. The Km and kcat values of this enzyme for trans-2'-carboxybenzalpyruvate were 50 microM and 13 s(-1), r ...[more]