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Literature summary extracted from

  • Mertsalov, I.B.; Novikov, B.N.; Scott, H.; Dangott, L.; Panin, V.M.
    Characterization of Drosophila CMP-sialic acid synthetase activity reveals unusual enzymatic properties (2016), Biochem. J., 473, 1905-1916 .
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.43 0.41
-
 N-acetylneuraminic acid at pH 8.0 and 37°C Drosophila melanogaster
2.7.7.43 0.45
-
 CTP at pH 8.0 and 37°C Drosophila melanogaster
2.7.7.43 3.5
-
 N-glycolneuraminate at pH 8.0 and 37°C Drosophila melanogaster

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.7.43 Golgi apparatus
-
 Drosophila melanogaster 5794
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.43 Co2+ the enzyme can function with a broad range of metal cofactors like Zn2+, Fe2+, Co2+ and Mn2+ Drosophila melanogaster
2.7.7.43 Fe2+ the enzyme can function with a broad range of metal cofactors like Zn2+, Fe2+, Co2+ and Mn2+ Drosophila melanogaster
2.7.7.43 Mg2+ the activity of the enzyme with Mg2+ is low, 20 mM Mg2+ is used in assay conditions Drosophila melanogaster
2.7.7.43 Mn2+ the enzyme can function with a broad range of metal cofactors like Zn2+, Fe2+, Co2+ and Mn2+ Drosophila melanogaster
2.7.7.43 Zn2+ the enzyme can function with a broad range of metal cofactors like Zn2+, Fe2+, Co2+ and Mn2+ Drosophila melanogaster

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.43 CTP + N-acetylneuraminic acid Drosophila melanogaster
-
 diphosphate + CMP-N-acetylneuraminic acid
-
 ?
2.7.7.43 CTP + sialic acid Drosophila melanogaster
-
 diphosphate + CMP-sialic acid
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.43 Drosophila melanogaster Q8IQV0
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.43 anti-FLAG affinity bead chromatography Drosophila melanogaster

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.43 CTP + N-acetylneuraminic acid
-
 Drosophila melanogaster diphosphate + CMP-N-acetylneuraminic acid
-
 ?
2.7.7.43 CTP + N-acetylneuraminic acid the enzyme displays specificity for N-acetylneuraminic acid as a substrate Drosophila melanogaster diphosphate + CMP-N-acetylneuraminic acid
-
 ?
2.7.7.43 CTP + N-glycolneuraminate relatively inferior substrate Drosophila melanogaster diphosphate + CMP-N-glycolneuraminate
-
 ?
2.7.7.43 CTP + sialic acid
-
 Drosophila melanogaster diphosphate + CMP-sialic acid
-
 ?
2.7.7.43 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

EC Number Subunits Comment Organism
2.7.7.43 ? x * 35000, SDS-PAGE Drosophila melanogaster

Synonyms

EC Number Synonyms Comment Organism
2.7.7.43 CMAS
-
 Drosophila melanogaster
2.7.7.43 CMP-Sia synthetase
-
 Drosophila melanogaster
2.7.7.43 CMP-sialic acid synthetase
-
 Drosophila melanogaster
2.7.7.43 CSAS
-
 Drosophila melanogaster
2.7.7.43 cytidine monophosphate N-acetylneuraminic acid synthetase
-
 Drosophila melanogaster

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.7.43 45
-
-
 Drosophila melanogaster

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.7.7.43 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.43 8
-
-
 Drosophila melanogaster

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.7.7.43 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