Abstract：
:Tritiated sodium borohydride was used to reduce the substrates of triosephosphate isomerase in the presence of the enzyme, and the mixture of the four possible products (D-[1(R)-3H]; D-[1(S)-3H]-; D-[2-3H]-, and L-[2-3H]glycerol 3-phosphate) was analyzed. While enzyme-bound dihydroxyacetone phosphate is reduced completely stereoselectively and at a rate eight imes faster than in free solution, D-glyceraldehyde 3-phosphate is inaccessible to reduction by borohydride when bound to the active site of the enzyme.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Webb MR,Knowles JRdoi
10.1021/bi00692a020subject
Has Abstractpub_date
1975-10-21 00:00:00pages
4692-8issue
21eissn
0006-2960issn
1520-4995journal_volume
14pub_type
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