1.3.99.4: 3-oxosteroid 1-dehydrogenase
This is an abbreviated version!
For detailed information about 3-oxosteroid 1-dehydrogenase, go to the full flat file.
Word Map on EC 1.3.99.4
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1.3.99.4
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rhodococcus
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3-ketosteroids
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mycobacterium
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cholesterol
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4-androstene-3,17-dione
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erythropolis
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synthesis
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arthrobacter
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simplex
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isoenzymes
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testosteroni
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rhodochrous
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androst-4-ene-3,17-dione
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bioconversion
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hydrocortisone
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dehydrogenation
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phytosterols
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ruber
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steroid-transforming
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globiformis
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1,4-androstadiene-3,17-dione
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neoaurum
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molecular biology
- 1.3.99.4
- rhodococcus
- 3-ketosteroids
- mycobacterium
- cholesterol
- 4-androstene-3,17-dione
- erythropolis
- synthesis
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arthrobacter
- simplex
- isoenzymes
- testosteroni
- rhodochrous
- androst-4-ene-3,17-dione
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bioconversion
- hydrocortisone
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dehydrogenation
- phytosterols
- ruber
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steroid-transforming
- globiformis
- 1,4-androstadiene-3,17-dione
- neoaurum
- molecular biology
Reaction
Synonyms
1-ene-dehydrogenase, 3-keto-5alpha-steroid DELTA(1)-dehydrogenase, 3-ketosteroid 1(2)-dehydrogenase, 3-ketosteroid delta1-dehydrogenase, 3-ketosteroid-1-en-dehydrogenase, 3-ketosteroid-D1-dehydrogenase, 3-ketosteroid-DELTA1-dehydrogenase, 3-ketosteroid-DELTA1-dehydrogenases, 3-oxosteroid D1-dehydrogenase, 3-oxosteroid Delta1-dehydrogenase, 3-oxosteroid:(2,6-dichlorphenolindophenol) DELTA1-oxidoreductase, 3-oxosteroid:(2,6-dichlorphenolindophenol)D1-oxidoreductase, 4-en-3-oxosteroid:(acceptor)-1-en-oxido-reductase, 4-ene-3-oxosteroid: (acceptor)-1-ene-oxoreductase, 4-ene-3-oxosteroid:(acceptor)l-ene-oxidoreductase, AcmB, AcmB2, cholest-4-en-3-one DELTA1-dehydrogenase, D1-dehydrogenase, D1-steroid reductase, dehydrogenase, 3-oxo steroid Delta 1-, Delta1-dehydrogenase, DELTA1-KstD, DELTA1-KSTD1, DELTA1-KstDA, DELTA1-KstDR, DELTA1-steroid reductase, ketosteroid DELTA1-dehydrogenase, KsdD, KsdD1, KsdD2, KsdD3, KsdD5, KsdDM, KSDH, KstD, KSTD1, KSTD2, KSTD3, KSTD3 orthologue, KstDF, MnKstD1, MnKstD2, MsKstD1, MsKstD2, MsKstD3, MsKstD4, ReKstD1, Rv3537, steroid-1-dehydrogenase
ECTree
1.3.99.4 3-oxosteroid 1-dehydrogenaseAdvanced search results
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Engineering on EC 1.3.99.4 - 3-oxosteroid 1-dehydrogenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
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
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
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
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
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
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
S138A
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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
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Y122F
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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
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Y125F
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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
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Y365F
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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
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S138A
Mycolicibacterium neoaurum TCCC 11028
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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
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Y122F
Mycolicibacterium neoaurum TCCC 11028
-
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
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Y125F
Mycolicibacterium neoaurum TCCC 11028
-
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
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Y365F
Mycolicibacterium neoaurum TCCC 11028
-
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
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G532A
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site-directed mutagenesis, the mutant shows over 70% reduced activity compare to wild-type enzyme
R256H
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site-directed mutagenesis, the mutant shows over 70% reduced activity compare to wild-type enzyme
Y355A
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site-directed mutagenesis, the mutant shows over 70% reduced activity compare to wild-type enzyme
additional information
additional information
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enzyme from strain ST-095 only differs in residue V366 from strain JC-12 (S366). Mutation results in almost 3fold higher catalytic efficiency in strain JC-12
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
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
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
additional information
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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
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
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
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
additional information
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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
additional information
enzyme mutants are constructed based on in silico protein docking modeling using site-directed mutagenesis and exogenous expression
additional information
Mycolicibacterium neoaurum DSM 1381
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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
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additional information
Mycolicibacterium neoaurum DSM 1381
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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
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additional information
-
enzyme from strain ST-095 only differs in residue V366 from strain JC-12 (S366). Mutation results in almost 3fold higher catalytic efficiency in strain JC-12
-
additional information
-
enzyme mutants are constructed based on in silico protein docking modeling using site-directed mutagenesis and exogenous expression
-
additional information
Mycolicibacterium neoaurum ST-095
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enzyme from strain ST-095 only differs in residue V366 from strain JC-12 (S366). Mutation results in almost 3fold higher catalytic efficiency in strain JC-12
-
additional information
Mycolicibacterium neoaurum TCCC 11028
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enzyme mutants are constructed based on in silico protein docking modeling using site-directed mutagenesis and exogenous expression
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additional information
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targeted disruption of the MSMEG5898 (ksdD-1) gene, but not the MSMEG4855 (ksdD-2) gene, results in partial inactivation of the cholesterol degradation pathway and accumulation of the intermediate 4-androstene-3,17-dione, reversible by the introduction of the wild-type ksdD-1 gene into deltaksdD-1 or overexpression of ksdD-2
additional information
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
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targeted disruption of the MSMEG5898 (ksdD-1) gene, but not the MSMEG4855 (ksdD-2) gene, results in partial inactivation of the cholesterol degradation pathway and accumulation of the intermediate 4-androstene-3,17-dione, reversible by the introduction of the wild-type ksdD-1 gene into deltaksdD-1 or overexpression of ksdD-2
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additional information
development of a synthetic 3-ketosteroid DELTA1-dehydrogenase (DELTA1-KstDR) for the generation of a catabolic pathway enabling cholesterol degradation in human cells. Coexpression with cholesterol-3-hydroxy-dehydrogenase (CholD) and 3-oxosteroid-9alpha-hydroxylase (Kst-9alphaH). CholD activity catalyzes the generation of a C-3 ketone, which is needed for DELTA1-KstD activity, which introduces a double bond between the C-1 and C-2 atoms of 3-oxosteroids. Cholesterol catabolism pathway in Actinomycetes, overview. The downstream enzymes need to have equal or greater activity when compared to the enzymes acting upstream to allow the pathway to flow and to prevent the accumulation of toxic intermediates, kinetic study
additional information
development of a synthetic 3-ketosteroid DELTA1-dehydrogenase (DELTA1-KstDA) for the generation of a catabolic pathway enabling cholesterol degradation in human cells. Coexpression with cholesterol-3-hydroxy-dehydrogenase (CholD) and 3-oxosteroid-9alpha-hydroxylase (Kst-9alphaH). CholD activity catalyzes the generation of a C-3 ketone, which is needed for DELTA1-KstD activity, which introduces a double bond between the C-1 and C-2 atoms of 3-oxosteroids. Cholesterol catabolism pathway in Actinomycetes, overview
