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Literature summary extracted from

  • Qiu, J.; Zang, S.; Ma, Y.; Owusu, L.; Zhou, L.; Jiang, T.; Xin, Y.
    Homology modeling and identification of amino acids involved in the catalytic process of Mycobacterium tuberculosis serine acetyltransferase (2017), Mol. Med. Rep., 15, 1343-1347 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.30 gene CysE, sequence comparisons, recombinant expression of wild-type and mutant C-terminally His-tagged enzymes in Escherichia coli strain BL21(DE3) Mycobacterium tuberculosis

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.30 D67A site-directed mutagenesis, the mutant shows 9.79% activity compared to wild-type enzyme Mycobacterium tuberculosis
2.3.1.30 H117A site-directed mutagenesis, the mutant shows 20.82% activity compared to wild-type enzyme Mycobacterium tuberculosis
2.3.1.30 H82A site-directed mutagenesis, the mutant shows 14.31% activity compared to wild-type enzyme Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.30 acetyl-CoA + L-serine Mycobacterium tuberculosis
-
 CoA + O-acetyl-L-serine
-
 ?
2.3.1.30 acetyl-CoA + L-serine Mycobacterium tuberculosis H37Rv
-
 CoA + O-acetyl-L-serine
-
 ?
2.3.1.30 acetyl-CoA + L-serine Mycobacterium tuberculosis ATCC 25618
-
 CoA + O-acetyl-L-serine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.30 Mycobacterium tuberculosis P95231
-
-
2.3.1.30 Mycobacterium tuberculosis ATCC 25618 P95231
-
-
2.3.1.30 Mycobacterium tuberculosis H37Rv P95231
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.30 recombinant wild-type and mutant His-tagged enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.30 acetyl-CoA + L-serine
-
 Mycobacterium tuberculosis CoA + O-acetyl-L-serine
-
 ?
2.3.1.30 acetyl-CoA + L-serine
-
 Mycobacterium tuberculosis H37Rv CoA + O-acetyl-L-serine
-
 ?
2.3.1.30 acetyl-CoA + L-serine
-
 Mycobacterium tuberculosis ATCC 25618 CoA + O-acetyl-L-serine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.30 ? x * 23770, sequence calculation, x * 30000, recombinant wild-type and mutant enzymes, SDS-PAGE Mycobacterium tuberculosis
2.3.1.30 More homology modeling of the enzyme's three-dimensional structure using the protein structure 3P47A of the A-chain of Entamoeba histolytica CysE (refined at a resolution of 1.78 A) as template, the CysE protein possesses a left-handed-beta-helix domain, overview Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
2.3.1.30 CysE
-
 Mycobacterium tuberculosis
2.3.1.30 serine acetyltransferase
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.30 37
-
 assay at Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.30 8
-
 assay at Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.30 acetyl-CoA
-
 Mycobacterium tuberculosis

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.3.1.30 Mycobacterium tuberculosis sequence calculation
-
 7.11

General Information

EC Number General Information Comment Organism
2.3.1.30 evolution enzyme CysE belongs to the hexaxadpeptide acetyltransferase family, characterized by imperfect tandem repeats of the hexapeptide motif [LIV]-[GAED]-X2-[STAV]-X Mycobacterium tuberculosis
2.3.1.30 additional information homology modeling and identification of amino acids involved in the catalytic process. The conserved amino acid residues D67, H82 and H117 may be involved in the catalytic activity and, thus, the function of CysE Mycobacterium tuberculosis