Any feedback?
Literature summary for 2.7.7.51 extracted from
- Adenylylsulfate-ammonia adenylyltransferase from Chlorella (1987), Methods Enzymol., 143, 354-361.
No PubMed abstract available
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.82 | - |
adenylylsulfate | - |
Auxenochlorella pyrenoidosa |  |
| 10 | - |
ammonia | - |
Auxenochlorella pyrenoidosa | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 17000 | - |
1 * 26000 + 1 * 21000 + 1 * 17000, SDS-PAGE | Auxenochlorella pyrenoidosa |
| 21000 | - |
1 * 26000 + 1 * 21000 + 1 * 17000, SDS-PAGE | Auxenochlorella pyrenoidosa |
| 26000 | - |
1 * 26000 + 1 * 21000 + 1 * 17000, SDS-PAGE | Auxenochlorella pyrenoidosa |
| 60000 | 65000 | PAGE | Auxenochlorella pyrenoidosa |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| adenylylsulfate + NH3 | Escherichia coli | the product adenosine 5'-phosphoramidate replaces AMP as an activator of phosphorylase b, threonine dehydratase and adenylate cyclase | adenosine 5'-phosphoramidate + sulfate | - |
? | |
| adenylylsulfate + NH3 | Hordeum vulgare | the product adenosine 5'-phosphoramidate replaces AMP as an activator of phosphorylase b, threonine dehydratase and adenylate cyclase | adenosine 5'-phosphoramidate + sulfate | - |
? | |
| adenylylsulfate + NH3 | Spinacia oleracea | the product adenosine 5'-phosphoramidate replaces AMP as an activator of phosphorylase b, threonine dehydratase and adenylate cyclase | adenosine 5'-phosphoramidate + sulfate | - |
? | |
| adenylylsulfate + NH3 | Dictyostelium discoideum | the product adenosine 5'-phosphoramidate replaces AMP as an activator of phosphorylase b, threonine dehydratase and adenylate cyclase | adenosine 5'-phosphoramidate + sulfate | - |
? | |
| adenylylsulfate + NH3 | Auxenochlorella pyrenoidosa | the product adenosine 5'-phosphoramidate replaces AMP as an activator of phosphorylase b, threonine dehydratase and adenylate cyclase | adenosine 5'-phosphoramidate + sulfate | - |
? | |
| adenylylsulfate + NH3 | Euglena sp. | the product adenosine 5'-phosphoramidate replaces AMP as an activator of phosphorylase b, threonine dehydratase and adenylate cyclase | adenosine 5'-phosphoramidate + sulfate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Auxenochlorella pyrenoidosa | - |
- |
- |
| Dictyostelium discoideum | - |
- |
- |
| Escherichia coli | - |
- |
- |
| Euglena sp. | - |
- |
- |
| Hordeum vulgare | - |
- |
- |
| Spinacia oleracea | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Auxenochlorella pyrenoidosa |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Auxenochlorella pyrenoidosa |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| adenylylsulfate + NH3 | very high specificity for the adenylylsulfate and ammonia | Escherichia coli | adenosine 5'-phosphoramidate + sulfate | - |
? | |
| adenylylsulfate + NH3 | very high specificity for the adenylylsulfate and ammonia | Hordeum vulgare | adenosine 5'-phosphoramidate + sulfate | - |
? | |
| adenylylsulfate + NH3 | very high specificity for the adenylylsulfate and ammonia | Spinacia oleracea | adenosine 5'-phosphoramidate + sulfate | - |
? | |
| adenylylsulfate + NH3 | very high specificity for the adenylylsulfate and ammonia | Dictyostelium discoideum | adenosine 5'-phosphoramidate + sulfate | - |
? | |
| adenylylsulfate + NH3 | very high specificity for the adenylylsulfate and ammonia | Auxenochlorella pyrenoidosa | adenosine 5'-phosphoramidate + sulfate | - |
? | |
| adenylylsulfate + NH3 | very high specificity for the adenylylsulfate and ammonia | Euglena sp. | adenosine 5'-phosphoramidate + sulfate | - |
? | |
| adenylylsulfate + NH3 | the product adenosine 5'-phosphoramidate replaces AMP as an activator of phosphorylase b, threonine dehydratase and adenylate cyclase | Escherichia coli | adenosine 5'-phosphoramidate + sulfate | - |
? | |
| adenylylsulfate + NH3 | the product adenosine 5'-phosphoramidate replaces AMP as an activator of phosphorylase b, threonine dehydratase and adenylate cyclase | Hordeum vulgare | adenosine 5'-phosphoramidate + sulfate | - |
? | |
| adenylylsulfate + NH3 | the product adenosine 5'-phosphoramidate replaces AMP as an activator of phosphorylase b, threonine dehydratase and adenylate cyclase | Spinacia oleracea | adenosine 5'-phosphoramidate + sulfate | - |
? | |
| adenylylsulfate + NH3 | the product adenosine 5'-phosphoramidate replaces AMP as an activator of phosphorylase b, threonine dehydratase and adenylate cyclase | Dictyostelium discoideum | adenosine 5'-phosphoramidate + sulfate | - |
? | |
| adenylylsulfate + NH3 | the product adenosine 5'-phosphoramidate replaces AMP as an activator of phosphorylase b, threonine dehydratase and adenylate cyclase | Auxenochlorella pyrenoidosa | adenosine 5'-phosphoramidate + sulfate | - |
? | |
| adenylylsulfate + NH3 | the product adenosine 5'-phosphoramidate replaces AMP as an activator of phosphorylase b, threonine dehydratase and adenylate cyclase | Euglena sp. | adenosine 5'-phosphoramidate + sulfate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| trimer | 1 * 26000 + 1 * 21000 + 1 * 17000, SDS-PAGE | Auxenochlorella pyrenoidosa |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Auxenochlorella pyrenoidosa |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.8 | - |
- |
Auxenochlorella pyrenoidosa |
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
