EC Number |
General Information |
Reference |
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3.1.1.58 | physiological function |
A pdi disruption mutant is attenuated for virulence in the hybrid striped bass model and for survival in whole fish blood. Pdi promotes bacterial resistance to lysozyme killing and the ability to adhere to and invade epithelial cells. There is no difference in the autolytic potential, resistance to oxidative killing or resistance to cationic antimicrobial peptides between Streptococcus iniae wild-type and pdi disruption mutant |
709850 |
3.1.1.58 | more |
structure determination and analysis using a molecular replacement procedure, method overview. Contruction of putative models of the C-terminal domain of the protein using a multitude of homology-modelling algorithms, and test for the presence of signal in molecular replacement calculations, slow-cooling torsion-angle simulated annealing |
-, 728874 |
3.1.1.58 | evolution |
the enzyme belongs to the bacterial family 4 carbohydrate esterases (CE-4) found whose members contain a conserved (alpha/beta)8 fold |
728915 |
3.1.1.58 | evolution |
the enzyme belongs to the family 4 carbohydrate esterases, CE4 |
729238 |
3.1.1.58 | malfunction |
enzyme deletion causes dramatically reduced biofilm formation in vitro as well as reduced pathogenicity in animal models of biofilm infections |
729238 |
3.1.1.58 | more |
the metal-dependent enzyme has a conserved His-His-Asp catalytic triad |
729238 |
3.1.1.58 | evolution |
conservation of holdfast synthesis genes in the Caulobacterales clade of the Alphaproteobacteria, gene hfsH is broadly conserved in the hfs gene cluster across several bacterial species |
730413 |
3.1.1.58 | malfunction |
disruption of the hfsH gene, which encodes a putative polysaccharide deacetylase, leads to accumulation of polar polysaccharide holdfast in the culture supernatant. The hfsH deletion mutant strain synthesizes holdfast, but the holdfasts are shed into the medium and have decreased adhesiveness and cohesiveness, phenotype, overview. Site-directed mutagenesis at the predicted catalytic site D48 phenocopied the DELTAhfsH mutant and abolishes the esterase activity of the enzyme |
730413 |
3.1.1.58 | malfunction |
disruption of the hfsH gene, which encodes a putative polysaccharide deacetylase, leads to accumulation of polar polysaccharide holdfast in the culture supernatant. The hfsH deletion mutant strain synthesizes holdfast, but the holdfasts are shed into the medium and have decreased adhesiveness and cohesiveness, phenotype, overview. Site-directed mutagenesis at the predicted catalytic site phenocopied the DELTAhfsH mutant and abolishes the esterase activity of the enzyme |
730413 |
3.1.1.58 | more |
the HfsH protein contains 4 conserved motifs, including the essential acetate binding residues and the zinc-binding triad, the enzyme has all the known essential components required to function as polysaccharide deacetylase |
730413 |