5.4.2.12	D12N	no activity	650970	
5.4.2.12	D319A	site-directed mutagenesis, substitution of the metal-binding residue Asp319 by Ala results in complete loss of independent PGAM activity	727472	
5.4.2.12	H123N	3% of wild-type activity	650970	
5.4.2.12	H125N	67% of wild-type activity	650970	
5.4.2.12	H128N	20% of wild-type activity	650970	
5.4.2.12	H23A	no enzymic activity. Like wild-type, mutant forms a dimer	679715	
5.4.2.12	H407N	no activity	650970	
5.4.2.12	H42N	91% of wild-type activity	650970	
5.4.2.12	H42N/H128N	8% of wild-type activity	650970	
5.4.2.12	H445N	18% of wild-type activity	650970	
5.4.2.12	H462N	0.3% of wild-type activity	650970	
5.4.2.12	H66N	2% of wild-type activity	650970	
5.4.2.12	additional information	down-regulation of enzyme steady state levels by RNAi correlates with a marked reduction of enzyme activity. Enzyme is required for cell growth in procyclic Trypanosoma brucei	682237	
5.4.2.12	additional information	insertional mutants of PMG1 and duble mutants of PMG1 and PMG2 are generated. While single mutants are indistinguishable from wild-type in all plant phenotypes assayed, double mutants have no detectable iPGAM activity and show defects in blue light-, abscisic acid-, and low CO2-regulated stomatal movements	728053	
5.4.2.12	additional information	reduction of enzyme activity by RNA interference leads to embroynic lethality, larval lethylity, and abnormal body morphology	662259	
5.4.2.12	R261L	no activity	650970	
5.4.2.12	S62A	no activity	650970	
5.4.2.12	S62A	no phosphoglycerate mutase activity	652915