The serine acetyltransferase reaction: acetyl transfer from an acylpantothenyl donor to an alcohol

Indigenous proteases in the skin of unicorn leatherjacket (Alutherus monoceros) and their influence on characteristic and functional properties of gelatin

“…PMSF irreversibly inhibits serine proteases by sulphonylation of the serine residue in the active site of the protease (James, 1978). The active site in each serine protease includes a serine residue, a histidine residue, and an aspartate residue (Johnson, Roderick, & Cook, 2005). Therefore, it can be inferred that a serine protease was the major protease associated with unicorn leatherjacket pretreated skin.…”

A Mechanistic Model of the Cysteine Synthase Complex

“…Cysteine biosynthesis involves a bienzyme complex, termed the CS complex, which is composed of homohexameric SAT and homodimeric OAS-TL enzymes. [11][12][13][14][15][16][17][18] Crystallographic data for the individual structures of SAT and OAS-TL from bacteria and OAS-TL from A. thaliana cytosol are available, but no structure of a plant SAT or the CS complex is available. [19][20][21][22][23][24][25][26][27][28][29] A detailed study of protein-protein interactions revealed that the C-terminus of SAT plays a crucial role in the association of SAT and OAS-TL.…”

Dominant-Negative Modification Reveals the Regulatory Function of the Multimeric Cysteine Synthase Protein Complex in Transgenic Tobacco

“…By contrast, Cys synthesis occurs in plastids, the cytosol, and mitochondria of most cells and in most plant species. It is performed by a protein system of compartment-specific isoforms with reversible quaternary structure (for reviews, see Droux, 2004;Wirtz et al, 2004;Johnson et al, 2005). Serine acetyltransferase (SAT) is assumed to consist of a dimer of homotrimers that only forms O-acetylserine (OAS) from Ser and acetyl-CoA with highest efficiency if it is associated with two homodimers of O-acetylserine (thiol) lyase (OAS-TL) in the Cys synthase complex (CSC).…”