Production and properties of adhesin-free gingipain proteinase RgpA.

ABSTRACT: The Arg-specific gingipains of Porphyromonas gingivalis RgpA and RgpB have 97% identical sequences in their catalytic domains yet their propeptides are only 76% identical. RgpA isolates as a proteinase-adhesin complex (HRgpA) which hinders direct kinetic comparison of RgpA_cat as a monomer with monomeric RgpB. We tested modifications of rgpA identifying a variant that enabled us to isolate histidine-tagged monomeric RgpA (rRgpAH). Kinetic comparisons between rRgpAH and RgpB used benzoyl-L-Arg-4-nitroanilide with and without cysteine and glycylglycine acceptor molecules. With no glycylglycine, values of K_m, V_max, k_cat and k_cat/K_m for each enzyme were similar, but with glycylglycine K_m decreased, V_max incr

SUBMITTER: Mahmud ASM 

PROVIDER: S-EPMC10319874 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature