in general, neutral-active or reproductive hyaluronidases, i.e. hyases, exemplified by sperm adhesion molecule 1, SPAM1, are responsible for hyaluronan digestion in the egg vestments and for sperm-zona binding, but murine SPAM1 has acidic activity. Presence of HYAL3 in mouse sperm where it contributes to hyase activity at pH 3, 4 and 7 as well as to cumulus penetration and the induction of the acrosome reaction
in general, neutral-active or reproductive hyaluronidases, i.e. hyases, exemplified by sperm adhesion molecule 1, SPAM1, are responsible for hyaluronan digestion in the egg vestments and for sperm-zona binding. Presence of HYAL3 in human sperm where it contributes to hyase activity at pH 3, 4 and 7 as well as to cumulus penetration and the induction of the acrosome reaction
hyaluronate lyase is proposed to be one of the key bacteriophage-encoded virulence factors. The Gly-X-Y motif of HylP has a regulatory role for enzyme function
bacterium employs two distinct variants of hyaluronan lyases. Variant HYL-IB/II is highly active, resulting in complete hyaluronan degradation. It is present in strains of the phylotypes IB and II. Variant HYL-IA has low activity, resulting in incomplete hyaluronan degradation. It is present in type IA strains. Type IA strains are primarily found on the skin surface and associated with acne vulgaris, type IB/II strains are more often associated with soft and deep tissue infections
loss of hylB or/and constitutively expressed hylZ has no significant effects on cell growth, lactic acid, and hyaluronan yields. The HylB mutant strain produces hyaluronan with an 18 % increase in molecular weight
presence of a hot spot region (A144GVVVY149) towards the carboxy terminus of isoform HylP2, which is essential for the acceleration of fibril formation. The hot spot is inherently mutated for valines (A178AMVMY183) in case of isoform HylP. The N-terminal swapped chimeras between these phage hyaluronan lyases (N-HylP2-C-HylP and N-HylP-C-HylP2) or HylP do not form fibrils at acidic pH. Seeding of prefibrils of HylP2 recompenses nucleation and leads to fibrillation in N-HylP-C-HylP2. The V147A mutation in the hot spot region abolishes fibril formation in HylP2. The M179V and M181V double mutations in the hot spot region of HylP leads to fibrillation with the seeding of prefibrils. Fibrillation in isoform HylP2 is initiated by the N-terminus, but may be accelerated by the conserved hot spot region in the C-terminus. A collagenous (Gly-X-Y)10 motif in the N-terminus and a mutated hot spot region in the C-terminus of isoform HylP affect fibrillar nucleation and acceleration, respectively
screening of 50 isolates from the three major clonal complexes found in North America (sequence types ST 1, ST25, and ST28) known to differ in their degree of virulence. All but one ST1 isolates (high virulence) are devoid of hyaluronate lyase activity whereas all ST25 (intermediate virulence) and ST28 (low virulence) isolates possess the activity
complete catalytic cycle for the degradation of hyaluronan tetrasaccharide catalyzed by the hyaluronate lyase from Spectrococcus pneumonia, overview. Active site residue is tyrosine 408. Quantum mechanical/molecular mechanical and desity calculation and modeling using truncated active site models
The primary catalytic residues of the enzyme seem to be in the first pocket consisting of Asp170 and Tyr182. Catalytic residues span between the regions containing 135-308 amino acids where both the catalytic pocket has a prominent positively charged residue, structure overview. The collagenous Gly-X-Y motif of the enzyme influences stability and interact with calcium ions suggesting its role in the enzyme regulation
The primary catalytic residues of the enzyme seem to be in the first pocket consisting of Asp170 and Tyr182. Catalytic residues span between the regions containing 135-308 amino acids where both the catalytic pocket has a prominent positively charged residue, structure overview. The collagenous Gly-X-Y motif of the enzyme influences stability and interact with calcium ions suggesting its role in the enzyme regulation