autocatalysis

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autocatalysis

[¦ōd·ō·kə′tal·ə·səs]
(chemistry)
A catalytic reaction started by the products of a reaction that was itself catalytic.
McGraw-Hill Dictionary of Scientific & Technical Terms, 6E, Copyright © 2003 by The McGraw-Hill Companies, Inc.
References in periodicals archive ?
PARs are members of the G-protein-coupled family, seven-transmembrane domain receptors, and their activation occurs through proteolytic cleavage of the N-terminal domain by proteinases, leading to the generation of a new N-terminal "tethered ligand," which binds to the receptor itself resulting in its autoactivation [1, 2].
Puente, "Autoactivation and environmental regulation of bfpT expression, the gene coding for the transcriptional activator of bfpA in enteropathogenic Escherichia coli," Molecular Microbiology, vol.
Preparation of Recombinant Legumain in Pichia pastoris and Autoactivation. We overexpressed human legumain proenzyme, which is reported to cleave ProT[alpha] at asparaginyl-glycine sites and release peptide products T[alpha]1 and T[alpha]11, in Pichiapastoris, and purified it by cation exchange chromatography.
(170) Receptor tyrosine kinases contain a YXXXYY motif within the activation loop of their kinase domains, and phosphorylation of these tyrosines is essential for autoactivation and induction of downstream signaling.
A single nucleotide polymorphism of CYP2B6 found in Japanese enhances catalytic activity by autoactivation. Biochem Biophys Res Commun 2001;281:1256-60.
The modeled GRN includes Oct4-Sox2 heterodimer autoactivation and its activation on Nanog; also, as in Kalmar's model, Nanog autoactivation is considered (Figure 3(b)).
This myeloproliferative syndrome is characterized by erythroid cells displaying deregulated proliferation due to a mutation (V617F) in the signaling protein JAK2, inducing autoactivation of this kinase by autophosphorylation [43].
Some PRSS1 gene mutations appear to increase the stability of the trypsin protein by eliminating a trypsin autodegradation site while other PRSS1 gene mutations appear to enhance trypsinogen autoactivation, both of which eventually result in chronic pancreatitis.
N-Terminal sequencing data further confirmed the production of the pro-form of hK4 (Gly-Ser-Cys-Ser-Gln-Ile-Ile-Asn-GlyGlu) with 5 additional amino acids (activation peptide) at the N[H.sub.2] terminus (underlined), suggesting the absence of autoactivation.