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CagA modulates host cell iron homeostasis and fundamental metabolic functions of the bacterial cell, promoting the synthesis of polyunsaturated ether phospholipids (PUFA-ePLs) through increased expression of alkylglycerone phosphate synthase and 1-acylglycerol-3-phosphate O-acyltransferase 3, resulting in susceptibility to ferroptosis in GC cells [49]

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Compared to the ~1000-fold decrease for alanine racemase and the 260-fold decrease for O-acetylserine sulfhydrylase, 10 9 -fold is very large.[68] The fact that AAT suffers such a large decrease in activity from changing the pyridine nitrogen to carbon, while that for alanine racemase is only ~10 3 -fold and that for O-acetylserine sulfhydrylase even less, strongly supports the proposal that not all PLP enzymes need to, or necessarily should, strongly stabilize the carbanionic intermediate by protonation of the pyridine nitrogen

Diabetes 35, 8996