EC Number |
General Information |
Reference |
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6.3.1.20 | evolution |
lipoate protein ligase 1 (PfLipL1) is an ATP-dependent ligase that belongs to the biotin/lipoate A/B protein ligase family (PFAM PF03099) |
746406 |
6.3.1.20 | malfunction |
LplA1 knockout cannot be achieved because of the essential function of the gene/protein in asexual parasite growth |
706425 |
6.3.1.20 | malfunction |
LplA1-cKO parasites shows severely impaired growth in vivo in the first 8 days of infection, and retarded blood-stage development in vitro, in the absence of ATc. But these parasites resume viability in the late stage of infection and mounted high levels of parasitemia leading to the death of the hosts. The lplA2 gene can be activated as an alternative pathway to compensate for the loss of LplA1 activity and to maintain lipoic acid metabolism |
-, 745964 |
6.3.1.20 | malfunction |
LplA1Ct is able to complement an Escherichia coli LplA knockout mutant at an efficiency of 94% |
725251 |
6.3.1.20 | metabolism |
LplA1 plays a critical role for asexual parasite growth in vitro and in vivo. |
706425 |
6.3.1.20 | metabolism |
LplA1 plays a pivotal role during the development of the erythrocytic stages of the malaria parasite. |
706425 |
6.3.1.20 | metabolism |
The LipB octanoyltransferase catalyzes the first step of lipoic acid synthesis in Escherichia coli, transfer of the octanoyl moiety from octanoyl-acyl carrier protein to the lipoyl domains of the E2 subunits of the 2-oxoacid dehydrogenases of aerobic metabolism. |
704311 |
6.3.1.20 | physiological function |
although lplA1 mRNA expression is regulated tightly by anhydrotetracycline (ATc) during the whole course of infection, lplA2 mRNA expression is significantly increased in the late stage of infection only in the LplA1-cKO parasites that are not exposed to anhydrotetracycline |
-, 745964 |
6.3.1.20 | physiological function |
although lplA1 mRNA expression is regulated tightly by anhydrotetracycline (ATc) during the whole course of infection, lplA2 mRNA expression is significantly increased in the late stage of infection only in the LplA1-cKO parasites that are not exposed to anhydrotetracycline. The lplA2 gene can be activated as an alternative pathway to compensate for the loss of LplA1 activity and to maintain lipoic acid metabolism |
-, 745964 |
6.3.1.20 | physiological function |
enzyme LplA naturally catalyzes the ligation of lipoic acid to the free epsilon-amino moiety of a lysine residue in the specific LAP sequence |
744699 |