Brown H M, Rejda J M, Chollet R
Biochim Biophys Acta. 1980 Aug 7;614(2):545-52. doi: 10.1016/0005-2744(80)90243-0.
Hydroxylamine directly and reversibly inhibits both activities of homogeneous ribulose-1,5-bisphosphate carboxylase-oxygenase (3-phospho-D-glycerate carboxy-lyase (dimerizing), EC 4.1.1.39) isolated from diverse sources. NH2OH is an uncompetitive inhibitor of carboxylase activity with respect to ribulose-bisphosph ate. This reagent also reacts non-enzymically with ribulosebisphosphate to deplete this substrate. Contrary to previous reports, these results indicate that hydroxylamine directly and indirectly inhibits both activities of this bifunctional enzyme.
羟胺能直接且可逆地抑制从不同来源分离得到的纯态核酮糖-1,5-二磷酸羧化酶加氧酶（3-磷酸-D-甘油酸羧基裂解酶（二聚化），EC 4.1.1.39）的两种活性。对于羧化酶活性而言，NH2OH是相对于核酮糖二磷酸的非竞争性抑制剂。该试剂还能与核酮糖二磷酸发生非酶反应，从而消耗这种底物。与之前的报道相反，这些结果表明羟胺能直接和间接抑制这种双功能酶的两种活性。
