1.2.1.13	A(plusCTE)	chimeric mutant for testing the regulatory function of CTE	676575	
1.2.1.13	B(E326Q)	site specific mutant of the GAPDH B-subunit	676575	
1.2.1.13	B(minCTE)	deletion mutant for testing the regulatory function of CTE	676575	
1.2.1.13	B(R77A)	site specific mutant of the GAPDH B-subunit	676575	
1.2.1.13	B(S188A)	site specific mutant of the GAPDH B-subunit	676575	
1.2.1.13	C151S	mutant, substituting Ser for Cys at position 151 of GAPDH results in no binding to the cells, no decreased cell-spreading efficiency and no cell morphological changes	672334	
1.2.1.13	C18S	mutant of GapB subunit still shows stron redox regulation	656096	
1.2.1.13	C274S	mutant of GapB subunit still shows stron redox regulation	656096	
1.2.1.13	C285S	mutant of GapB subunit still shows stron redox regulation	656096	
1.2.1.13	C349S	mutant of GapB subunit is less redox-sensitive than GapB. Active tetramer, unable to aggregate to higher oligomers in presence of NAD+	656096	
1.2.1.13	C349S/C358S	mutant of GapB subunit is less redox-sensitive than GapB. Active tetramer, unable to aggregate to higher oligomers in presence of NAD+	656096	
1.2.1.13	c358S	mutant of GapB subunit is less redox-sensitive than GapB. Active tetramer, unable to aggregate to higher oligomers in presence of NAD+	656096	
1.2.1.13	D351N	the mutation only marginally affects the redox sensitivity	689747	
1.2.1.13	E356Q	the mutation only marginally affects the redox sensitivity	689747	
1.2.1.13	E356Q/E357Q	complete redox insensitivity is achieved in the double mutant	689747	
1.2.1.13	E357Q	the mutation only marginally affects the redox sensitivity	689747	
1.2.1.13	K128A	Km-value for NADPH is nearly identical to wild-type value, turnover-number for NADPH is decreased about 2fold. Km-value for NADH is increased 2.1fold compared to wild-type enzyme, turnover-number for NADH is decreased 2.6fold	655492	
1.2.1.13	K128E	Km-value for NADPH is about 80% of the wild-type value, turnover-number for NADPH is decreased 2.7fold. Km-value for NADH is increased 2.3fold compared to wild-type enzyme, turnover-number for NADH is decreased 1.9fold	655492	
1.2.1.13	K225A	K225 is critical for binding of GAPDH to Siah1, an ubiquitin-E3-ligase, eliciting the translocation of GAPDH to the nucleus	676851	
1.2.1.13	additional information	construction of hybrid enzymes between the glyceraldehyde-3-phosphate dehydrogenases from the mesophilic Methanobacterium bryantii and the thermophilic Methanothermus fervidus	287989	
1.2.1.13	additional information	to increase NADPH bioavailability, the native NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase (GAPDH) gapA gene, EC 1.2.1.12, in Escherichia coli is replaced with the NADP+-dependent gapB gene, EC 1.2.1.13, from Bacillus subtilis. To overcome the limitation of NADP+ availability, Escherichia coli NAD kinase, gene nadK is also coexpressed with gapB in Escherichia coli. replacing NAD+-dependent GapA activity with NADP+-dependent GapB activity increases the synthesis of NADPH-dependent compounds	-, 743027	
1.2.1.13	R190A	the catalytic constant, kcat, of the mutant in the presence of NADH decreases 10fold while the Km for NADH decreases 12fold. The mutant shows no activity with NADPH	724306	
1.2.1.13	R197A	Km-value for NADPH is identical to wild-type value, turnover-number for NADPH is about 90% of the wild-type value. Km-value for NADH is about 80% of the wild-type value, turnover-number for NADH is nearly identical to wild-type value	655492	
1.2.1.13	R197E	Km-value for NADPH is increased 1.3fold compared to wild-type enzyme, turnover-number for NADPH is decreased 2fold. Km-value for NADH is about 90% of the wild-type value, turnover-number for NADH is increased 1.3fold	655492	
1.2.1.13	R82A	the mutation leads to a 10fold increase in the Km for NADPH but does not affect the kinetics of NADH	724306	
1.2.1.13	R82D	the mutation leads to a 10fold increase in the Km for NADPH but does not affect the kinetics of NADH	724306	
1.2.1.13	S188A	affinity for NADPH is significantly decreased, decrease in the ratio of turnover number to Km-value in the NADPH-dependent reaction, significant expansion of the A4-tetramer	656539	
1.2.1.13	S195A	the mutation has no effect on the affinity of the enzyme for NADPH and its affinity for NADH and for BPGA in the presence of NADH is reduced	724306	
1.2.1.13	T33A	affinity for NADPH is significantly decreased, turnover-number for NADPH is lowered	656539	
1.2.1.13	T33A/S188A	affinity for NADPH is significantly decreased, turnover-number for NADPH is lowered	656539	
1.2.1.13	Y123W	increase of temperature of irreversible inactivation by 1.3°C	287989	
1.2.1.13	Y323S	decrease of temperature of irreversible inactivation by 4.5°C	287989