Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Lrhorfi, L.A.; Srinivasan, G.V.; Schauer, R.
    Properties and partial purification of sialate-O-acetyltransferase from bovine submandibular glands (2007), Biol. Chem., 388, 297-306.
    View publication on PubMed

General Stability

EC Number General Stability Organism
2.3.1.45 Neu5Ac or CMP-Neu5Ac are strongly required for stabilization of the solubilized enzyme during purification Bos taurus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.45 CoA competitive inhibitor; strong product inhibition Bos taurus
2.3.1.45 KCl activates, optimally at 50 mM, 80% inhibition at 500 mM Bos taurus
2.3.1.45 additional information no inhibition by AMP, CMP, EDTA and DTT Bos taurus
2.3.1.45 NaCl 50% inhibition at 50 mM Bos taurus
2.3.1.45 Zn2+ 50% inhibition at 1 mM Bos taurus
2.3.1.45 ZnCl2 50% inhibition at 1 mM Bos taurus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.45 additional information
-
additional information kinetics for the solubilized and the membrane-bound enzyme at different conditions, overview Bos taurus
2.3.1.45 0.0073
-
CMP-N-acetylneuraminic acid pH 6.5, 37°C, solubilized enzyme Bos taurus
2.3.1.45 0.008
-
acetyl-CoA pH 6.5, 37°C, solubilized enzyme Bos taurus
2.3.1.45 0.0084
-
acetyl-CoA
-
Bos taurus
2.3.1.45 0.1285
-
CMP-N-acetylneuraminic acid
-
Bos taurus
2.3.1.45 0.1385
-
N-acetylneuraminic acid
-
Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.45 membrane
-
Bos taurus 16020
-
2.3.1.45 microsome
-
Bos taurus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.1.45 KCl activates, optimally at 50 mM for the solubilized enzyme and at 70 mM for the membrane-bound enzyme, 80% inhibition at 500 mM Bos taurus
2.3.1.45 KCl optimum activity at 50 mM Bos taurus
2.3.1.45 additional information the enzyme is not affected Mn2+, Ca2+, and Mg2+ Bos taurus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.45 150000
-
between 150000-160000 Da, determined by gel filtration Bos taurus
2.3.1.45 150000 160000 gel filtration Bos taurus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.45 additional information Bos taurus the O-acetylation of sialic acids in various positions is a frequent modification of these residues in glycoproteins and glycolipids, sialic acid O-acetylation is involved in the regulation of many cell biological and pathophysiological events ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.45 Bos taurus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.45 native enzyme 53fold, partially, from microsomes by solubilization with the zwitterionic detergent CHAPS, i.e. 3-[(3-cholamidopropyl)dimethylammonio]-1-propane sulfonic acid, dialysis, anion exchange chromatography, and two steps of CoA affinity chromatography Bos taurus
2.3.1.45 using gel filtration, ion exchange chromatography, and affinity chromatography Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.45 submandibular gland
-
Bos taurus
-

Storage Stability

EC Number Storage Stability Organism
2.3.1.45 -20°C, partially purified solubilized enzyme, 2 weeks, loss of 25% activity Bos taurus
2.3.1.45 -80°C, partially purified solubilized and membrane-bound enzyme, stable for several months Bos taurus
2.3.1.45 -80°C, stable for several months Bos taurus
2.3.1.45 22°C, room temperature, partially purified solubilized enzyme, almost complete loss of activity within a few hours Bos taurus
2.3.1.45 4°C, partially purified solubilized enzyme, 8 h, quite stable Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.45 acetyl-CoA + CMP-N-acetylneuraminic acid best substrate Bos taurus CoA + CMP-N-acetyl-9-O-acetyl-neuraminate the 9-O-acetylsialic acid is the main product ?
2.3.1.45 acetyl-CoA + N-acetylneuraminic acid
-
Bos taurus CoA + N-acetyl-9-O-acetyl-neuraminate the 9-O-acetylsialic acid is the main product ?
2.3.1.45 CMP-N-acetylneuraminic acid + acetyl-CoA
-
Bos taurus CoA + CMP-5-N-acetyl-9-O-acetyl neuraminic acid
-
?
2.3.1.45 additional information the O-acetylation of sialic acids in various positions is a frequent modification of these residues in glycoproteins and glycolipids, sialic acid O-acetylation is involved in the regulation of many cell biological and pathophysiological events Bos taurus ?
-
?
2.3.1.45 additional information substrate specificity, overview, no involvement of an isomerase in the migration of O-acetyl groups within the sialic acid side chain, at pH 9.5 in buffer only, a significant proportion of Neu5,7Ac2 is converted non-enzymatically to Neu5,9Ac within 15 min Bos taurus ?
-
?
2.3.1.45 N-acetylneuraminic acid + acetyl-CoA
-
Bos taurus CoA + 5-N-acetyl-9-O-acetyl neuraminic acid
-
?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.45 sialate O-acetyltransferase
-
Bos taurus
2.3.1.45 sialate-O-acetyltransferase
-
Bos taurus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.45 37
-
-
Bos taurus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.3.1.45 additional information
-
the solubilised enzyme loses approximately 25% of its activity after 2 weeks at -20°C. It is also stable at 48°C for 8 h, but loses most of its activity at room temperature within a few hours Bos taurus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.45 6.5
-
-
Bos taurus
2.3.1.45 6.5
-
solubilized enzyme Bos taurus
2.3.1.45 7.5
-
membrane-bound enzyme Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.45 acetyl-CoA
-
Bos taurus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.3.1.45 0.02
-
CoA
-
Bos taurus
2.3.1.45 0.02
-
CoA pH 7.5, 37°C, microsome-bound enzyme Bos taurus