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Inter-domain communication of human cystathionine beta-synthase: structural basis of S-adenosyl-l-methionine activation

In accordance with the glutathione activator hypothesis, only positively charged amino acids replace Lys105 in enzymatically active glutaredoxins, whereas in inactive isoforms and other members of the thioredoxin superfamily the activator candidate is often separated from the catalytic cysteine residue in the primary sequence or is replaced by uncharged residues 3,11,12 (Fig

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Subcellular localization of a plant catalase-phenol oxidase, AcCATPO, from Amaranthus and identification of a non-canonical peroxisome targeting signal

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