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Literature summary for 3.2.1.35 extracted from
- High-yield recombinant expression of the extremophile enzyme, bee hyaluronidase in Pichia pastoris (2008), Protein Expr. Purif., 57, 226-233.
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | this recombinant hyaluronidase can be applied for biochemical or medical purposes | Apis mellifera |
| medicine | this recombinant hyaluronidase can be applied for biochemical or medical purposes | synthetic construct |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Pichia pastoris strain GS115 | Apis mellifera |
| expression in Pichia pastoris GS115, expression vector pPIC9, together with human serum albumin, expression in Escherichia coli BL21 DE3, vector pMW172, fusion protein | Apis mellifera |
| using the information of preferred Pichia pastoris codons as provided by Genscript, Inc., the native sequence is de novo synthesized to create a fully codon-optimized cDNA (Hya delta c) and the synthetic gene is expressed in Pichia | synthetic construct |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | after expression of a fusion protein by linking hyaluronidase and human serum albumin together with the recognition sequence for the protease, factorXa, fragmented protein products are obtained in the culture supernatant, only after replacement of the hinge region with a serine-glycine-rich linker, stable full-length fusion protein could be generated | Apis mellifera |
| additional information | after expression of a fusion protein by linking hyaluronidase and human serum albumin together with the recognition sequence for the protease, factorXa, fragmented protein products are obtained in the culture supernatant, only after replacement of the hinge region with a serine-glycine-rich linker, stable full-length fusion protein could be generated | synthetic construct |
| additional information | when changing the codons of the original transcript to triplet sequences preferred by Pichia pastoris, no further increase of protein product can be achieved | Apis mellifera |
| additional information | when changing the codons of the original transcript to triplet sequences preferred by Pichia pastoris, no further increase of protein product can be achieved | synthetic construct |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Apis mellifera | Q08169 | expression in Pichia pastoris GS115, expression vector pPIC9, together with human serum albumin, expression in Escherichia coli BL21 DE3, vector pMW172, fusion protein | - |
| Apis mellifera | Q08169 | hyaluronoglucosaminidase precursor | - |
| synthetic construct | EU152302 | using the information of preferred Pichia pastoris codons as provided by Genscript, Inc., the native sequence is de novo synthesized to create a fully codon-optimized cDNA (Hya delta c) and the synthetic gene is expressed in Pichia | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| by ion exchange chromatography at pH 5.0 | Apis mellifera |
| by ion exchange chromatography at pH 5.0 | synthetic construct |
| HiTrap HP SP column chromatography | Apis mellifera |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| culture supernatant | - |
Apis mellifera | - |
| venom | - |
Apis mellifera | - |
| venom gland | - |
Apis mellifera | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.0000245 | - |
recombinant enzyme from crude extract, in 100 mM sodium phosphate, pH 5.0, at 37°C | Apis mellifera |
| 0.000239 | - |
recombiannt enzyme after 9.6fold purification, in 100 mM sodium phosphate, pH 5.0, at 37°C | Apis mellifera |
| 0.49 | - |
culture supernatant | Apis mellifera |
| 0.49 | - |
culture supernatant | synthetic construct |
| 4.77 | - |
ion exchange | Apis mellifera |
| 4.77 | - |
ion exchange | synthetic construct |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-S-chondroitin sulfate + H2O | - |
Apis mellifera | ? | - |
? |  |
| 4-S-chondroitin sulfate + H2O | - |
synthetic construct | ? | - |
? | |
| 6-S-chondroitin sulfate + H2O | the enzyme is capable of degrading chondroitin sulfate C at a rate of around 40% compared to its hyaluronidase activity | Apis mellifera | ? | - |
? | |
| 6-S-chondroitin sulfate + H2O | the enzyme is capable of degrading CS-C at a rate of around 40% compared to its hyaluronidase activity | synthetic construct | ? | - |
? | |
| chondroitin B sulfate + H2O | very little hydrolase activity towards chondroitin sulfate B (dermatan sulfate) | Apis mellifera | ? | - |
? | |
| chondroitin sulfate A + H2O | - |
Apis mellifera | ? | - |
? | |
| chondroitin sulfate B + H2O | very little hydrolase activity | Apis mellifera | ? | - |
? | |
| chondroitin sulfate B + H2O | very little hydrolase activity | synthetic construct | ? | - |
? | |
| chondroitin sulfate C + H2O | - |
Apis mellifera | ? | - |
? | |
| hyaluronan + 2 H2O | - |
Apis mellifera | N-acetyl-beta-D-glucosamine + D-glucuronate + ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Hyal | - |
Apis mellifera |
| hyaluronidase | - |
Apis mellifera |
| hyaluronidase | - |
synthetic construct |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 62 | - |
- |
Apis mellifera |
| 62 | - |
- |
synthetic construct |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 4 | 90 | - |
Apis mellifera |
| 4 | 90 | 34% activity at temperatures as low as 4°C still exhibits hydrolase activity at 90°C to an extent of 19% in comparison to the optimum | Apis mellifera |
| 4 | 90 | 34% activity at temperatures as low as 4°C still exhibits hydrolase activity at 90°C to an extent of 19% in comparison to the optimum | synthetic construct |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 4 | 90 | 34% activity at temperatures as low as 4°C still exhibits hydrolase activity at 90°C to an extent of 19% in comparison to the optimum | Apis mellifera |
| 4 | 90 | 34% activity at temperatures as low as 4°C still exhibits hydrolase activity at 90°C to an extent of 19% in comparison to the optimum | synthetic construct |
| 90 | - |
19% activity at 90°C | Apis mellifera |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 3.8 | - |
- |
Apis mellifera |
| 3.8 | - |
- |
synthetic construct |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 3 | 8 | - |
Apis mellifera |
| 3 | 8 | native and the recombinant enzyme are active at extreme conditions | Apis mellifera |
| 3 | 8 | native and the recombinant enzyme are active at extreme conditions | synthetic construct |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 3 | 8 | native and recombinant enzyme exhibit activity | Apis mellifera |
| 3 | 8 | native and recombinant enzyme exhibit activity | synthetic construct |
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