PURIFICATION AND PROPERTIES OF SERINE HYDROXYMETHYLTRANSFERASE FROM NICOTIANA RUSTICA L.

Serine hydroxymethyltransferase was partially purified fromNicotiana rustica roots. The pH optimum for the enzyme is 4.0.A requirement for pyridoxal phosphate and a divalent cationwas shown, and the enzyme was inhibited by sulfhydryl reagentsand the reaction is folic acid-dependent. ¹Contribution from the Department of Biochemistry and publishedwith the approval of the Director of Research as Paper No. 2175in the Journal Series ²Present address; Spruance Research Laboratories, E. I. du Pontde Nemours and Company, Inc., Post Office Box 1477, Richmond,Virginia 23212, U.S.A.