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Literature summary for 4.2.2.1 extracted from
- Hyaluronidases: their genomics, structures, and mechanisms of action (2006), Chem. Rev., 106, 818-839.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure analysis | Streptococcus pneumoniae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| hyaluronan | Streptococcus pyogenes phage H4489A | absolute substrate specificity of the bacteriophage enzyme | hyaluronic acid oligomers | - |
? |  |
| hyaluronic acid | Streptococcus agalactiae | degradation | hyaluronic acid oligomers | - |
? | |
| hyaluronic acid | Streptococcus pneumoniae | degradation | hyaluronic acid oligomers | - |
? | |
| hyaluronic acid | Streptomyces hyalurolyticus | highly specific for hyaluronan, degradation, unsaturated products of varied size | hyaluronic acid oligomers | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptococcus agalactiae | - |
- |
- |
| Streptococcus pneumoniae | Q54873 | - |
- |
| Streptococcus pyogenes phage H4489A | - |
gene hylP | - |
| Streptomyces hyalurolyticus | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| [hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate | binding of negatively charged hydrophobic substrates is facilitated by the predominantly positive and hydrophobic cleft located at distorted (alpha/alpha)5-6 barrel, mechanism of hyaluronan degradation, active site residues are Asn349, His399, and Tyr408, overview | Streptococcus pneumoniae | |
| [hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate | binding of negatively charged hydrophobic substrates is facilitated by the predominantly positive and hydrophobic cleft located at distorted (alpha/alpha)5-6 barrel, mechanism of hyaluronan degradation, overview | Streptococcus agalactiae | |
| [hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate | mechanism of hyaluronan degradation, random endolytic action pattern, overview | Streptomyces hyalurolyticus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| commercial preparation | - |
Streptomyces hyalurolyticus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| hyaluronan | absolute substrate specificity of the bacteriophage enzyme | Streptococcus pyogenes phage H4489A | hyaluronic acid oligomers | - |
? | |
| hyaluronic acid | - |
Streptococcus agalactiae | hyaluronic acid oligomers | - |
? | |
| hyaluronic acid | - |
Streptococcus pneumoniae | hyaluronic acid oligomers | - |
? | |
| hyaluronic acid | degradation | Streptococcus agalactiae | hyaluronic acid oligomers | - |
? | |
| hyaluronic acid | degradation | Streptococcus pneumoniae | hyaluronic acid oligomers | - |
? | |
| hyaluronic acid | highly specific for hyaluronan, degradation, unsaturated products of varied size | Streptomyces hyalurolyticus | hyaluronic acid oligomers | - |
? | |
| hyaluronic acid | highly specific for hyaluronan | Streptomyces hyalurolyticus | hyaluronic acid oligomers | primarily disaccharides, but also tetrasaccharides and hexasaccharides | ? | |
| additional information | the enzyme also catalyzes the degradation of other polymeric glycans | Streptococcus agalactiae | ? | - |
? | |
| additional information | the enzyme also catalyzes the degradation of other polymeric glycans | Streptococcus pneumoniae | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | domain structure, overview | Streptomyces hyalurolyticus |
| More | the enzyme contains a distorted (alpha/alpha)5-6 barrel composed of alpha-helices inside and out, substrate binding is facilitated by the predominantly positive and hydrophobic cleft located at the top of the wider end of the barrel nested among helices and interhelix loops, domain structure, overview | Streptococcus agalactiae |
| More | the enzyme contains a distorted (alpha/alpha)5-6 barrel composed of alpha-helices inside and out, substrate binding is facilitated by the predominantly positive and hydrophobic cleft located at the top of the wider end of the barrel nested among helices and interhelix loops, domain structure, overview | Streptococcus pneumoniae |
| More | the enzyme is very short in sequence and different in structure compared to enzymes of other species | Streptococcus pyogenes phage H4489A |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Hyal | - |
Streptococcus agalactiae |
| Hyal | - |
Streptococcus pneumoniae |
| Hyal | - |
Streptococcus pyogenes phage H4489A |
| HylP | - |
Streptococcus pyogenes phage H4489A |
| More | the enzyme belongs to the CAZY polysaccharide lyase family 16 | Streptococcus pyogenes phage H4489A |
| More | the enzyme belongs to the polysaccharide lyase family 8 | Streptococcus agalactiae |
| More | the enzyme belongs to the polysaccharide lyase family 8 | Streptococcus pneumoniae |
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