STUDIES ON HOMOSERINE DEHYDROGENASE IN PEA SEEDLINGS |
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Authors: | SASAOKA KEI |
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Institution: | Laboratory of Amino Acid Chemistry, Research Institute for Food Science, Kyoto University |
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Abstract: | Partially purified homoserine dehydrogenase was prepared frompea seedlings. The optimum pH for this enzyme is approximately 5.4. The Kmvaluesfor ASA and TPNH are 4.6xl04Af and 7.7xl05M, respectively.This enzyme can also utilize DPNH but less effectively thanTPNH. In contrast with yeast homoserine dehydrogenase whichis insensitive to SH reagents, the pea enzyme is inhibitedalmost completely by 104MPCMB and 105MHgCl2, theinhibition being removed by 102M thioglycolate. Homoserinedehydrogenase was found not only in decotylized seedlings, butalso in cotyledons. The significance of this enzyme in homoserine biosynthesis ingerminating pea seeds has been discussed. (Received February 20, 1961; ) |
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