Transcriptomic changes of Corynebacterium glutamicum strain when deleted gdhA and expressing hemA

Glutamate dehydrogenase (GDH), was a key enzyme which catalyzes the conversion of ketoglutarate and ammonium to produce a large number of a large number of glutamate accumulation, which may consume massive NAD(P)H and carbon resource. The blocking of the glutamate synthesis pathway could re-allocate the carbon flux to produce 5-ALA. Transcriptomic changes were used to reveal the the mechanism for high 5-ALA yield of engineered C. glutamicum strain. Transcriptome sequencing of strains F1-P (A, C. glutamicum harboring pXMJ19), F1-A (B, C. glutamicum harboring pXMJ19-hemA), F2-A (C, C. glutamicum gdhA harboring pXMJ19-hemA), were performed when cultured for 32 h.