| Autor: |
Abu Sayeed M. Mahmud, Christine A. Seers, N. Laila Huq, Lianyi Zhang, Catherine A. Butler, Caroline Moore, Keith J. Cross, Eric C. Reynolds |
| Jazyk: |
angličtina |
| Rok vydání: |
2023 |
| Předmět: |
|
| Zdroj: |
Scientific Reports, Vol 13, Iss 1, Pp 1-12 (2023) |
| Druh dokumentu: |
article |
| ISSN: |
2045-2322 |
| DOI: |
10.1038/s41598-023-37534-x |
| Popis: |
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 RgpAcat 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 increased and k cat increased ~ twofold for RgpB but ~ sixfold for rRgpAH. The k cat/K m for rRgpAH was unchanged whereas that of RgpB more than halved. Recombinant RgpA propeptide inhibited rRgpAH and RgpB with K i 13 nM and 15 nM K i respectively slightly more effectively than RgpB propeptide which inhibited rRgpAH and RgpB with K i 22 nM and 29 nM respectively (p |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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