5.4.3.8	L-glutamate 1-semialdehyde	-	Arabidopsis thaliana	5-aminolevulinate	-	?	417145	
5.4.3.8	L-glutamate 1-semialdehyde	-	Pseudomonas aeruginosa	5-aminolevulinate	-	?	417145	
5.4.3.8	L-glutamate 1-semialdehyde	-	Corynebacterium glutamicum	5-aminolevulinate	-	?	417145	
5.4.3.8	L-glutamate 1-semialdehyde	-	Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025	5-aminolevulinate	-	?	417145	
5.4.3.8	L-glutamate 1-semialdehyde	-	Escherichia coli MG1655	5-aminolevulinate	-	?	417145	
5.4.3.8	L-glutamate 1-semialdehyde	-	Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1	5-aminolevulinate	-	?	417145	
5.4.3.8	additional information	complex formation between glutamyl-tRNA reductase and glutamate-1-semialdehyde 2,1-aminomutase in Escherichia coli during the initial reactions of porphyrin biosynthesis suggests direct metabolic channeling between both enzymes to protect the reactive aldehyde species glutamate-1-semialdehyde	Escherichia coli	?	-	?	89	
5.4.3.8	additional information	enzyme GSAM catalyzes the transamination of GSA substrate to form 5-aminolevulinate by an unusual intramolecular exchange of amino and oxo groups via the intermediate 4,5-diaminovalerate (DAVA). The reaction starts with imine formation between pyridoxamine 5'-phosphate and the aldehyde of GSA. During the first half of the reaction pyridoxamine 5'-phosphate is converted to pyridoxal 5'-phosphate, while pyridoxamine 5'-phosphate is regenerated in the second half of the reaction upon 5-aminolevulinate formation	Arabidopsis thaliana	?	-	?	89