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Literature summary for 1.3.99.4 extracted from

  • Zhang, R.; Liu, X.; Wang, Y.; Han, Y.; Sun, J.; Shi, J.; Zhang, B.
    Identification, function, and application of 3-ketosteroid DELTA1-dehydrogenase isozymes in Mycobacterium neoaurum DSM 1381 for the production of steroidic synthons (2018), Microb. Cell Fact., 17, 77 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.3.99.4

Cloned(Commentary)

Cloned (Comment) Organism
isozyme KstD1, DNA and amino acid sequence determination and analysis, sequence comparisons of isozyme KstD1-3 and other KstD enzymes, phylogenetic analysis, quantitative RT-PCR enzyme expression analysis, recombinant expression in Escherichia coli strain BL21(DE3) and Bacillus subtilis strain 6051a, subcloning in Escherichia coli strain DH5alpha, isozyme KstD1 overexpression in the DELTAkstD1 deletion mutant strain Mycolicibacterium neoaurum
isozyme KstD2, DNA and amino acid sequence determination and analysis, sequence comparisons of isozyme KstD1-3 and other KstD enzymes, phylogenetic analysis, quantitative RT-PCR enzyme expression analysis, recombinant expression in Escherichia coli strain BL21(DE3) and Bacillus subtilis strain 6051a, subcloning in Escherichia coli strain DH5alpha, isozyme KstD2 overexpression in the DELTAkstD1 deletion mutant strain Mycolicibacterium neoaurum
isozyme KstD3, DNA and amino acid sequence determination and analysis, sequence comparisons of isozyme KstD1-3 and other KstD enzymes, phylogenetic analysis, quantitative RT-PCR enzyme expression analysis, recombinant expression in Escherichia coli strain BL21(DE3) and Bacillus subtilis strain 6051a, subcloning in Escherichia coli strain DH5alpha, isozyme KstD3 overexpression in the DELTAkstD1 deletion mutant strain Mycolicibacterium neoaurum

Protein Variants

Protein Variants Comment Organism
additional information among the three KstD isozymes, KstD2 shows the highest enzymatic activity when expressed heterogeneously, and KstD1 performs poorly, especially in Escherichia coli. For isozyme KstD3, the KstD enzyme activities are hardly detected in either host, Escherichia coli or Bacillus subtilis Mycolicibacterium neoaurum
additional information construction of a kstD1 deletion mutant. Among the three KstD isozymes, KstD2 shows the highest enzymatic activity when expressed heterogeneously, and KstD1 performs poorly, especially in Escherichia coli. For isozyme KstD3, the KstD enzyme activities are hardly detected in either host, Escherichia coli or Bacillus subtilis Mycolicibacterium neoaurum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-androstene-3,17-dione + acceptor Mycolicibacterium neoaurum
-
 1,4-androstadiene-3,17-dione + reduced acceptor
-
 ?
4-androstene-3,17-dione + acceptor Mycolicibacterium neoaurum DSM 1381
-
 1,4-androstadiene-3,17-dione + reduced acceptor
-
 ?

Organism

Organism UniProt Comment Textmining
Mycolicibacterium neoaurum A0A2P1IUY8
-
-
Mycolicibacterium neoaurum A0A2P1IUZ1
-
-
Mycolicibacterium neoaurum A0A2P1IUZ5
-
-
Mycolicibacterium neoaurum DSM 1381 A0A2P1IUY8
-
-
Mycolicibacterium neoaurum DSM 1381 A0A2P1IUZ1
-
-
Mycolicibacterium neoaurum DSM 1381 A0A2P1IUZ5
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
22-hydroxy-23, 24-bisnorchola-4-en-3-one + 2,6-dichlorophenol-indophenol
-
 Mycolicibacterium neoaurum ? + reduced 2,6-dichlorophenol-indophenol
-
 ?
22-hydroxy-23, 24-bisnorchola-4-en-3-one + 2,6-dichlorophenol-indophenol
-
 Mycolicibacterium neoaurum DSM 1381 ? + reduced 2,6-dichlorophenol-indophenol
-
 ?
4-androstene-3,17-dione + 2,6-dichlorophenol-indophenol
-
 Mycolicibacterium neoaurum 1,4-androstadiene-3,17-dione + reduced 2,6-dichlorophenol-indophenol
-
 ?
4-androstene-3,17-dione + 2,6-dichlorophenol-indophenol
-
 Mycolicibacterium neoaurum DSM 1381 1,4-androstadiene-3,17-dione + reduced 2,6-dichlorophenol-indophenol
-
 ?
4-androstene-3,17-dione + acceptor
-
 Mycolicibacterium neoaurum 1,4-androstadiene-3,17-dione + reduced acceptor
-
 ?
4-androstene-3,17-dione + acceptor
-
 Mycolicibacterium neoaurum DSM 1381 1,4-androstadiene-3,17-dione + reduced acceptor
-
 ?
9,22-dihydroxy-23,24-bisnorchol-4-ene-3-one + 2,6-dichlorophenol-indophenol
-
 Mycolicibacterium neoaurum ? + reduced 2,6-dichlorophenol-indophenol
-
 ?
9alpha-hydroxy-4-androstene-3,17-dione + 2,6-dichlorophenol-indophenol
-
 Mycolicibacterium neoaurum 9alpha-hydroxy-1,4-androstadiene 3,17-dione + reduced 2,6-dichlorophenol-indophenol
-
 ?
9alpha-hydroxy-4-androstene-3,17-dione + 2,6-dichlorophenol-indophenol
-
 Mycolicibacterium neoaurum DSM 1381 9alpha-hydroxy-1,4-androstadiene 3,17-dione + reduced 2,6-dichlorophenol-indophenol
-
 ?
additional information among the three KstD isozymes, KstD2 shows the highest enzymatic activity when expressed heterogeneously, and KstD1 performs poorly, especially in Escherichia coli. For isozyme KstD3, the KstD enzyme activities are hardly detected in either host, Escherichia coli or Bacillus subtilis Mycolicibacterium neoaurum ?
-
-
additional information among the three KstD isozymes, KstD2 shows the highest enzymatic activity when expressed heterogeneously, and KstD1 performs poorly, especially in Escherichia coli. For isozyme KstD3, the KstD enzyme activities are hardly detected in either host, Escherichia coli or Bacillus subtilis Mycolicibacterium neoaurum DSM 1381 ?
-
-

Synonyms

Synonyms Comment Organism
3-ketosteroid-DELTA1-dehydrogenase
-
 Mycolicibacterium neoaurum
KstD
-
 Mycolicibacterium neoaurum
KSTD1
-
 Mycolicibacterium neoaurum
KSTD2
-
 Mycolicibacterium neoaurum
KSTD3
-
 Mycolicibacterium neoaurum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Mycolicibacterium neoaurum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Mycolicibacterium neoaurum

Cofactor

Cofactor Comment Organism Structure
2,6-dichlorophenolindophenol DCPIP Mycolicibacterium neoaurum

General Information

General Information Comment Organism
metabolism oxosteroid-DELTA1-dehydrogenase (KstD) is a key enzyme in the metabolic pathway for chemical modifications of steroid hormones, overview of proposed pathway for phytosterols degradation in mycobacteria Mycolicibacterium neoaurum