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Literature summary extracted from
- Streptococcus pneumoniae hyaluronate lyase: an overview (2004), Curr. Sci., 86, 285-295.
No PubMed abstract available
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.2.1 | additional information | the enzyme is synthesized as inactive zymogen in the cell and then secreted and activated by cleavage of the signal peptide | Streptococcus pneumoniae | |
| 4.2.2.1 | additional information | the enzyme is synthesized as inactive zymogen in the cell and then secreted and activated by cleavage of the signal peptide | Streptococcus agalactiae |
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 4.2.2.1 | medicine | the enzyme can be used as a vaccine | Streptococcus pneumoniae |
| 4.2.2.1 | pharmacology | the enzyme is a target for structure-based design of selective inhibitors as drugs in bacterial infection therapy | Streptococcus pneumoniae |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.2.2.1 | expression in Escherichia coli resulting in different protein sizes | Streptococcus pneumoniae |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.2.2.1 | H399A | the mutant enzyme shows 12% of wild-type enzyme activity | Streptococcus pneumoniae |
| 4.2.2.1 | additional information | mutation of the catalytic residues Asn429, His479, and Tyr488 inactivates the enzyme | Streptococcus agalactiae |
| 4.2.2.1 | N349A | the mutant enzyme shows 6% of wild-type enzyme activity | Streptococcus pneumoniae |
| 4.2.2.1 | N580G | the mutant enzyme shows 115% of wild-type enzyme activity | Streptococcus pneumoniae |
| 4.2.2.1 | R243V | the mutant enzyme shows 67% of wild-type enzyme activity | Streptococcus pneumoniae |
| 4.2.2.1 | Y408F | the mutant enzyme is inactive | Streptococcus pneumoniae |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 4.2.2.1 | cell surface | - |
Streptococcus pneumoniae | 9986 | - |
| 4.2.2.1 | cell surface | - |
Streptococcus agalactiae | 9986 | - |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 4.2.2.1 | 91000 | 107000 | the recombinantly expressed enzyme exists in different proteolytically fragmented forms of the full-length enzyme with Mr of 107 kDa | Streptococcus pneumoniae |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.2.1 | hyaluronan | Streptococcus pneumoniae | - |
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine | disaccharide unit | ir |  |
| 4.2.2.1 | hyaluronan | Streptococcus agalactiae | - |
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine | disaccharide unit | ir | |
| 4.2.2.1 | additional information | Streptococcus pneumoniae | the enzyme is involved in degradation of hyaluronate from connective host tissues to facilitate the host and specific tissue invasion by the bacterium, overview | ? | - |
? | |
| 4.2.2.1 | additional information | Streptococcus agalactiae | the enzyme is involved in degradation of hyaluronate from connective host tissues to facilitate the host and specific tissue invasion by the bacterium, overview | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.2.1 | Streptococcus agalactiae | - |
- |
- |
| 4.2.2.1 | Streptococcus pneumoniae | - |
- |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 4.2.2.1 | proteolytic modification | the enzyme is synthesized as inactive zymogen in the cell and then secreted and activated by cleavage of the signal peptide | Streptococcus agalactiae |
| 4.2.2.1 | proteolytic modification | the enzyme is synthesized as inactive zymogen int he cell and then secreted and activated by cleavage of the signal peptide | Streptococcus pneumoniae |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 4.2.2.1 | [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 | catalytic reaction mechanism and structural requirements, catalytic residues are Asn349, His399, and Tyr408 | Streptococcus pneumoniae | |
| 4.2.2.1 | [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 | catalytic reaction mechanism and structural requirements, catalytic residues are Asn429, His479, and Tyr488, a required hydrophobic patch is composed of residues Glu468, Asp478, and Thr480 | Streptococcus agalactiae |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.2.1 | hyaluronan | - |
Streptococcus pneumoniae | 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine | disaccharide unit | ir | |
| 4.2.2.1 | hyaluronan | - |
Streptococcus agalactiae | 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine | disaccharide unit | ir | |
| 4.2.2.1 | hyaluronan | substrate structure | Streptococcus pneumoniae | 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine | disaccharide unit | ir | |
| 4.2.2.1 | hyaluronan | substrate structure | Streptococcus agalactiae | 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine | disaccharide unit | ir | |
| 4.2.2.1 | additional information | the enzyme is involved in degradation of hyaluronate from connective host tissues to facilitate the host and specific tissue invasion by the bacterium, overview | Streptococcus pneumoniae | ? | - |
? | |
| 4.2.2.1 | additional information | the enzyme is involved in degradation of hyaluronate from connective host tissues to facilitate the host and specific tissue invasion by the bacterium, overview | Streptococcus agalactiae | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.2.2.1 | More | the three-dimensional enzyme structure contains a catalytic alpha-domain at the N-terminus and a C-terminal supportive cell-wall-anchoring beta-domain connected by a short peptide linker | Streptococcus pneumoniae |
| 4.2.2.1 | More | the three-dimensional enzyme structure contains a catalytic alpha-domain at the N-terminus and a C-terminal supportive cell-wall-anchoring beta-domain connected by a short peptide linker | Streptococcus agalactiae |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.2.2.1 | HL | - |
Streptococcus pneumoniae |
| 4.2.2.1 | HL | - |
Streptococcus agalactiae |
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Release 2023.1 (January 2023)
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