Any feedback?
Literature summary extracted from
- Characterization of hyaluronic acid specific hyaluronate lyase (HylP) from Streptococcus pyogenes (2014), Biochimie, 102, 203-210.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.2.2.1 | DNA and amino acid sequence determination and analysis, recombinant expression of wild-type and truncation and point mutant enzymes in Escherichia coli strain BL21(DE3) using plasmid pSF49 | Streptococcus pyogenes phage H4489A |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.2.2.1 | D170T | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Streptococcus pyogenes phage H4489A |
| 4.2.2.1 | additional information | construction of truncated mutants hylp255e1113 and hylp390e1113, HylP enzyme without internal Gly-X-Y motif | Streptococcus pyogenes phage H4489A |
| 4.2.2.1 | Q295E | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Streptococcus pyogenes phage H4489A |
| 4.2.2.1 | W19F | site-directed mutagenesis, denaturation profile with guanidinium hydrochloride is similar to the wild-type enzyme | Streptococcus pyogenes phage H4489A |
| 4.2.2.1 | Y182F | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Streptococcus pyogenes phage H4489A |
| 4.2.2.1 | Y298F | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Streptococcus pyogenes phage H4489A |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.2.1 | Ca2+ | interacts with the collagenous Gly-X-Y motif of the enzyme, activates up to 20 mM, but inhibits at higher concentrations, inactivation above 50 mM | Streptococcus pyogenes phage H4489A |  |
| 4.2.2.1 | L-ascorbate | noncompetitive inhibition, inhibition kinetics, overview. Residues involved in the binding of L-ascorbate are confined to HylP135-308 | Streptococcus pyogenes phage H4489A | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.2.2.1 | additional information | - |
additional information | Michaelis-Menten kinetics | Streptococcus pyogenes phage H4489A | |
| 4.2.2.1 | 0.285 | - |
hyaluronic acid | pH 6.0, 25°C, recombinant wild-type enzyme | Streptococcus pyogenes phage H4489A | |
| 4.2.2.1 | 0.305 | - |
hyaluronic acid | pH 6.0, 25°C, recombinant mutant Y298F | Streptococcus pyogenes phage H4489A | |
| 4.2.2.1 | 0.373 | - |
hyaluronic acid | pH 6.0, 25°C, recombinant mutant Q295E | Streptococcus pyogenes phage H4489A | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.2.1 | Ca2+ | interacts with the collagenous Gly-X-Y motif of the enzyme, activates up to 20 mM, but inhibits at higher concentrations | Streptococcus pyogenes phage H4489A | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 4.2.2.1 | 40000 | - |
3 * 40000, SDS-PAGE | Streptococcus pyogenes phage H4489A |
| 4.2.2.1 | 120000 | - |
recombinant enzyme, glutaraldehyde cross-linking | Streptococcus pyogenes phage H4489A |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.2.1 | Streptococcus pyogenes phage H4489A | P15316 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.2.2.1 | recombinant wild-type and mutant enzymes from Escherichia coli | Streptococcus pyogenes phage H4489A |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.2.1 | hyaluronic acid | the enzyme is a hyaluronic acid specific hyaluronate lyase showing ability to degrade hyaluronate to unsaturated disaccharide units | Streptococcus pyogenes phage H4489A | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.2.2.1 | More | extended trimeric conformation, homology modeling using the crystal structure of HylP1 from Streptococcus pyogenes SF370 (PDB ID-2C3F) as a template, domain structure, overview | Streptococcus pyogenes phage H4489A |
| 4.2.2.1 | trimer | 3 * 40000, SDS-PAGE | Streptococcus pyogenes phage H4489A |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.2.2.1 | HylP | - |
Streptococcus pyogenes phage H4489A |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.2.2.1 | 25 | - |
assay at | Streptococcus pyogenes phage H4489A |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.2.2.1 | 2.76 | - |
hyaluronic acid | pH 6.0, 25°C, recombinant mutant Q295E | Streptococcus pyogenes phage H4489A | |
| 4.2.2.1 | 4.29 | - |
hyaluronic acid | pH 6.0, 25°C, recombinant mutant Y298F | Streptococcus pyogenes phage H4489A | |
| 4.2.2.1 | 5.65 | - |
hyaluronic acid | pH 6.0, 25°C, recombinant wild-type enzyme | Streptococcus pyogenes phage H4489A | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.2.2.1 | 6 | - |
assay at | Streptococcus pyogenes phage H4489A |
IC50 Value
| EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
|---|---|---|---|---|---|---|
| 4.2.2.1 | 0.7 | - |
pH 6.0, 25°C, recombinant wild-type enzyme | Streptococcus pyogenes phage H4489A | L-ascorbate | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.2.2.1 | malfunction | the enzyme activity is considerably reduced with mutation in the second pocket consisting of Glu295 and Tyr298 | Streptococcus pyogenes phage H4489A |
| 4.2.2.1 | additional information | 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 | Streptococcus pyogenes phage H4489A |
| 4.2.2.1 | physiological function | 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 | Streptococcus pyogenes phage H4489A |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
