Co-overexpression of AtSHMT1 and AtFDH induces sugar synthesis and enhances the role of original pathways during formaldehyde metabolism in tobacco

Molecular cloning, characterization, and homology modeling of serine hydroxymethyltransferase from psychrophilic bacterium Psychrobacter sp.

“…In this study, the Gly–PLP sites of PsSHMT in Figure 1 were identified to be Ser34, Tyr54, Tyr64, Gly97, Ser98, His125, Asp200, His203, His228, Lys229, Arg235, and Arg361, which were different from the SHMT from Helicobacter pylori (Tyr52, Ser94, Ser96, Ser172, Asp197, His200, Gly256, and Gly257) [5]. And the active sites of PsSHMT were consistent with the SHMTs from Thermoplasma acidophilum [3] and E. coli [18].…”

“…It has been reported that SHMT (EC 2.1.2.1) is a pyridoxal 5ʹ‐phosphate (PLP)‐dependent enzyme which can catalyze a reversible reaction of 3‐hydroxy amino acids to an aldehyde and glycine (Gly) [2] and synthesize purine [1]. In addition, SHMTs can provide activated one‐carbon units required for the synthesis of nucleic acids, proteins, and numerous biological compounds [3] and participate in de novo synthesis of thymidylate in mammals [4] and photorespiration in plants [5]. SHMTs also contribute to the treatment of cancers [6] and the development of antibiotics [7].…”

Rootstock–scion exchanging mRNAs participate in the pathways of amino acid and fatty acid metabolism in cucumber under early chilling stress

“…SHMT participated in the photorespiration pathway of plant oxygen-containing photosynthetic organisms [ 77 ] and played a vital role in drought [ 78 ], high salinity [ 79 ], high Zn toxicity [ 76 ], and other abiotic stresses. AtSHMT1 was also involved in HCHO glycoassimilation [ 80 ]. Thus, we speculated that chilling-induced mobile CmoSHMT mRNA (CmoCh03G008930) may be involved in the mutual conversion of serine and glycine in grafted Csa, and promote photorespiration to enhance the tolerance of Csa to chilling stress.…”