SNZ3 Encodes a PLP Synthase Involved in Thiamine Synthesis in Saccharomyces cerevisiae

摘要

Pyridoxal 5′-phosphate (the active form of vitamin B6) is a cofactor that is important for a broad number of biochemical reactions and is essential for all forms of life. Organisms that can synthesize pyridoxal 5′-phosphate use either the deoxyxylulose phosphate-dependent or -independent pathway, the latter is encoded by a two-component pyridoxal 5′-phosphate synthase. Saccharomyces cerevisiae contains three paralogs of the two-component SNZ/SNO pyridoxal 5′-phosphate synthase. Past work identified the biochemical activity of , and provided in vivo data that was involved in pyridoxal 5′-phosphate biosynthesis. and were considered redundant isozymes and no growth condition requiring their activity was reported. Genetic data herein showed that either or are required for efficient thiamine biosynthesis in Saccharomyces cerevisiae. Further, or alone could satisfy the cellular requirement for pyridoxal 5′-phosphate (and thiamine), while was sufficient for pyridoxal 5′-phosphate synthesis only if thiamine was provided. qRT-PCR analysis determined that , are repressed ten-fold by the presence thiamine. In total, the data were consistent with a requirement for PLP in thiamine synthesis, perhaps in the enzyme, that could only be satisfied by or . Additional data showed that is a pyridoxal 5′-phosphate synthase in vitro and is sufficient to satisfy the pyridoxal 5′-phosphate requirement in Salmonella enterica when the medium has excess ammonia.