Any feedback?
Literature summary for 2.7.7.43 extracted from
- Characterization of Drosophila CMP-sialic acid synthetase activity reveals unusual enzymatic properties (2016), Biochem. J., 473, 1905-1916 .
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.41 | - |
N-acetylneuraminic acid | at pH 8.0 and 37°C | Drosophila melanogaster |  |
| 0.45 | - |
CTP | at pH 8.0 and 37°C | Drosophila melanogaster | |
| 3.5 | - |
N-glycolneuraminate | at pH 8.0 and 37°C | Drosophila melanogaster |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| Golgi apparatus | - |
Drosophila melanogaster | 5794 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | the enzyme can function with a broad range of metal cofactors like Zn2+, Fe2+, Co2+ and Mn2+ | Drosophila melanogaster | |
| Fe2+ | the enzyme can function with a broad range of metal cofactors like Zn2+, Fe2+, Co2+ and Mn2+ | Drosophila melanogaster | |
| Mg2+ | the activity of the enzyme with Mg2+ is low, 20 mM Mg2+ is used in assay conditions | Drosophila melanogaster | |
| Mn2+ | the enzyme can function with a broad range of metal cofactors like Zn2+, Fe2+, Co2+ and Mn2+ | Drosophila melanogaster | |
| Zn2+ | the enzyme can function with a broad range of metal cofactors like Zn2+, Fe2+, Co2+ and Mn2+ | Drosophila melanogaster | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| CTP + N-acetylneuraminic acid | Drosophila melanogaster | - |
diphosphate + CMP-N-acetylneuraminic acid | - |
? | |
| CTP + sialic acid | Drosophila melanogaster | - |
diphosphate + CMP-sialic acid | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Drosophila melanogaster | Q8IQV0 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| anti-FLAG affinity bead chromatography | Drosophila melanogaster |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| CTP + N-acetylneuraminic acid | - |
Drosophila melanogaster | diphosphate + CMP-N-acetylneuraminic acid | - |
? | |
| CTP + N-acetylneuraminic acid | the enzyme displays specificity for N-acetylneuraminic acid as a substrate | Drosophila melanogaster | diphosphate + CMP-N-acetylneuraminic acid | - |
? | |
| CTP + N-glycolneuraminate | relatively inferior substrate | Drosophila melanogaster | diphosphate + CMP-N-glycolneuraminate | - |
? | |
| CTP + sialic acid | - |
Drosophila melanogaster | diphosphate + CMP-sialic acid | - |
? | |
| additional information | ATP, GTP and UTP, along with CDP and CMP cannot be used as substrates. The enzyme has a nearly undetectable activity toward 2-keto-3-deoxynononic acid and 2-keto-3-deoxyoctonic acid while no activity is detected with 3-deoxy-D-manno-2-octulosonic acid | Drosophila melanogaster | ? | - |
- |
|
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 35000, SDS-PAGE | Drosophila melanogaster |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CMAS | - |
Drosophila melanogaster |
| CMP-Sia synthetase | - |
Drosophila melanogaster |
| CMP-sialic acid synthetase | - |
Drosophila melanogaster |
| CSAS | - |
Drosophila melanogaster |
| cytidine monophosphate N-acetylneuraminic acid synthetase | - |
Drosophila melanogaster |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | - |
- |
Drosophila melanogaster |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | 45 | the enzyme activity steadily increases with temperature from 20 C to 45 C by approximately an order of magnitude. The activity declines dramatically at temperatures above 45 C | Drosophila melanogaster |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
- |
Drosophila melanogaster |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | 9 | the enzyme has a relatively narrow optimum around pH 8.0. In standard assay conditions, the enzyme activity declines precipitously at lower pH, dropping to 20% around pH 7.4 and becoming practically negligible below pH 7.0. The enzyme activity also declines substantially but more gradually, losing around 50% at pH 9.0. The enzyme exhibits significant activity at pH 6.5 in the presence of Mn2+, Co2+, Zn2+, Fe2+ and Ni2+ | Drosophila melanogaster |
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
