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Literature summary for 1.3.99.4 extracted from

  • Qin, N.; Shen, Y.; Yang, X.; Su, L.; Tang, R.; Li, W.; Wang, M.
    Site-directed mutagenesis under the direction of in silico protein docking modeling reveals the active site residues of 3-ketosteroid-DELTA1-dehydrogenase from Mycobacterium neoaurum (2017), World J. Microbiol. Biotechnol., 33, 146 .
    View publication on PubMed
Search for more literature for 1.3.99.4

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Mycolicibacterium neoaurum

Protein Variants

Protein Variants Comment Organism
E140V site-directed mutagenesis, no significant change in enzyme expression is caused by the mutation, the mutant shows reduced activity with 4-androstene-3,17-dione compared to wild-type enzyme Mycolicibacterium neoaurum
additional information enzyme mutants are constructed based on in silico protein docking modeling using site-directed mutagenesis and exogenous expression Mycolicibacterium neoaurum
S138A site-directed mutagenesis, no significant change in enzyme expression is caused by the mutation, the mutant shows reduced activity with 4-androstene-3,17-dione compared to wild-type enzyme Mycolicibacterium neoaurum
Y122F site-directed mutagenesis, no significant change in enzyme expression is caused by the mutation, the mutant shows similar activity with 4-androstene-3,17-dione compared to wild-type enzyme Mycolicibacterium neoaurum
Y125F site-directed mutagenesis, no significant change in enzyme expression is caused by the mutation, the mutant shows highly reduced activity with 4-androstene-3,17-dione compared to wild-type enzyme Mycolicibacterium neoaurum
Y365F site-directed mutagenesis, no significant change in enzyme expression is caused by the mutation, the mutant shows highly reduced activity with 4-androstene-3,17-dione compared to wild-type enzyme Mycolicibacterium neoaurum
Y472F site-directed mutagenesis, no significant change in enzyme expression is caused by the mutation, the mutant shows similar activity with 4-androstene-3,17-dione compared to wild-type enzyme Mycolicibacterium neoaurum
Y541F site-directed mutagenesis, no significant change in enzyme expression is caused by the mutation, the mutant shows highly reduced activity with 4-androstene-3,17-dione compared to wild-type enzyme Mycolicibacterium neoaurum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-androstene-3,17-dione + FAD Mycolicibacterium neoaurum
-
 1,4-androstadiene-3,17-dione + FADH2
-
 ?
4-androstene-3,17-dione + FAD Mycolicibacterium neoaurum MNR
-
 1,4-androstadiene-3,17-dione + FADH2
-
 ?
4-androstene-3,17-dione + FAD Mycolicibacterium neoaurum TCCC 11028
-
 1,4-androstadiene-3,17-dione + FADH2
-
 ?

Organism

Organism UniProt Comment Textmining
Mycolicibacterium neoaurum C6KID9
-
-
Mycolicibacterium neoaurum MNR C6KID9
-
-
Mycolicibacterium neoaurum TCCC 11028 C6KID9
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-androstene-3,17-dione + FAD
-
 Mycolicibacterium neoaurum 1,4-androstadiene-3,17-dione + FADH2
-
 ?
4-androstene-3,17-dione + FAD residues Y122, Y125, S138, E140, and Y541 from the FAD-binding domain and Y365 from the catalytic domain play a key role in this reaction Mycolicibacterium neoaurum 1,4-androstadiene-3,17-dione + FADH2
-
 ?
4-androstene-3,17-dione + FAD
-
 Mycolicibacterium neoaurum MNR 1,4-androstadiene-3,17-dione + FADH2
-
 ?
4-androstene-3,17-dione + FAD residues Y122, Y125, S138, E140, and Y541 from the FAD-binding domain and Y365 from the catalytic domain play a key role in this reaction Mycolicibacterium neoaurum MNR 1,4-androstadiene-3,17-dione + FADH2
-
 ?
4-androstene-3,17-dione + FAD
-
 Mycolicibacterium neoaurum TCCC 11028 1,4-androstadiene-3,17-dione + FADH2
-
 ?
4-androstene-3,17-dione + FAD residues Y122, Y125, S138, E140, and Y541 from the FAD-binding domain and Y365 from the catalytic domain play a key role in this reaction Mycolicibacterium neoaurum TCCC 11028 1,4-androstadiene-3,17-dione + FADH2
-
 ?

Synonyms

Synonyms Comment Organism
3-ketosteroid-DELTA1-dehydrogenases
-
 Mycolicibacterium neoaurum
KsdD
-
 Mycolicibacterium neoaurum

Cofactor

Cofactor Comment Organism Structure
FAD required Mycolicibacterium neoaurum

General Information

General Information Comment Organism
additional information enzyme residues Y125, Y365, and Y541 are essential to the function of KsdD, residues Y122, S138, and E140 contribute to the catalysis of KsdD, modelling of the enzyme-substrate bindung structure, overview Mycolicibacterium neoaurum