NAD+ and NADP+ can be used as cofactors with similar efficiency, unlike EC 18.104.22.168 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) and EC 22.214.171.124 glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating), which are NAD+- and NADP+-dependent, respectively.
Valverde, F., Losada, M. and Serrano, A. Cloning by functional complementation in E. coli of the gap2 gene of Synechocystis PCC 6803 supports an amphibolic role for cyanobacterial NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase. In: P. Mathis (Ed.), Photosynthesis: From Light to Biosphere, vol. 1, Kluwer Academic Publishers, 1995, pp. 959–962.
Valverde, F., Losada, M. and Serrano, A. Functional complementation of an Escherichia coli gap mutant supports an amphibolic role for NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase of Synechocystis sp. strain PCC 6803. J. Bacteriol.179 (1997) 4513–4522. [PMID: 9226260]