Premium
Arguments against a close relationship between non‐phosphorylating and phosphorylating glyceraldehyde‐3‐phosphate dehydrogenases
Author(s) -
Michels S.,
Scagliarini S.,
Seta F.Della,
Carles C.,
Riva M.,
Trost P.,
Branlant G.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80393-5
Subject(s) - phosphorylation , glyceraldehyde , glyceraldehyde 3 phosphate dehydrogenase , phosphate , chemistry , biochemistry , dehydrogenase , enzyme
Non‐phosphorylating NADP‐dependent glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH) (EC 1.2.1.9) from spinach leaves was purified to homogeneity using an improved purification procedure. Thus, a major contaminant with molecular mass and ion‐exchange properties similar to non‐phosphorylating GAPDH was eliminated. Using this pure non‐phosphorylating GAPDH, cofactor stereospecificity was determined by 1 H NMR. Analysis of the NADPH formed from the hydride transfer from glyceraldehyde‐3‐phosphate to [4‐ 2 H]NADP showed that the enzyme belongs to the A‐stereospecific dehydrogenase family. This stereospecificity is the same as that described for the aldehyde dehydrogenase (ALDH) superfamily and opposite to that of the phosphorylating GAPDH. Moreover, results from peptide sequencing analysis suggest a similarity in sequence between the non‐phosphorylating GAPDH and ALDHs. Thus, the results taken all together strongly suggest that non‐phosphorylating GAPDH belongs to the ALDH family and has no close relationship to the phosphorylating GAPDH class.