The amino acid sequence determines the characteristic folding patterns of the protein's structure, which is essential to enzyme specificity.
The results confirm the importance of residue M214 for donor enzyme specificity.
Comet parameters included: Trypsin enzyme specificity, semi-digested, allowed 1 missed cleavage, 50 ppm mass tolerance, cysteine modification of 57 Da (resulting from the iodoacetamide) and modifications on methionine of 15.999 Da (oxidation).
Factors including enzyme specificity, inhibitors, stability, and denaturation play vital roles in the rate of the enzymatic reactions.
Taken together, our data show that the enzyme specificity for cellular substrates and synthetic peptides differs for hPAD2 and hPAD4.
Also, crystal structures of complexes with AMP and UMP reveal the structural basis for the observed enzyme specificity.
These five residues occur in four short sequences conserved throughout the family, and within such sequences some key amino acid residues are related to enzyme specificity.
The EDGFFKI sequence also showed enzyme specificity for tissue TGase while no reaction was observed with plasma TGase (Factor XIIIa), consistent with its natural occurrence in vivo.
The effect of the modifications on the enzyme activity depends on the substrate and the reaction conditions: enzyme specificity is strongly altered by the chemical modification.
In general, the enzyme specificity of locust pacifastin-like inhibitors towards trypsin- or chymotrypsin-like peptidases corresponds to the nature of the P1-residue at the reactive site.
Mascot search parameters were as follows: enzyme specificity trypsin, fixed modifications cysteine carbamidomethylation, variable modification methionine oxidation.
