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Literature summary for 1.3.99.4 extracted from

  • Wojcik, P.; Glanowski, M.; Wojtkiewicz, A.M.; Rohman, A.; Szaleniec, M.
    Universal capability of 3-ketosteroid ?1-dehydrogenases to catalyze DELTA1-dehydrogenation of C17-substituted steroids (2021), Microb. Cell Fact., 20, 119 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.3.99.4

Activating Compound

Activating Compound Comment Organism Structure
2-hydroxypropyl-beta-cyclodextrin HBC, solubilizes and activates Rhodococcus erythropolis
2-hydroxypropyl-beta-cyclodextrin HBC, solubilizes and activates. The addition of solubilizing agent causes AcmB to exhibit a higher affinity to cholest-4-en-3-one than to 4-androstene-3,17-dione Sterolibacterium denitrificans

Application

Application Comment Organism
additional information 3-oxosteroid DELAT1-dehydrogenases are of particular interest for the etiology of some infectious diseases, for the production of starting materials for the pharmaceutical industry, and for environmental bioremediation applications Rhodococcus erythropolis
additional information 3-oxosteroid DELAT1-dehydrogenases are of particular interest for the etiology of some infectious diseases, for the production of starting materials for the pharmaceutical industry, and for environmental bioremediation applications Sterolibacterium denitrificans

Cloned(Commentary)

Cloned (Comment) Organism
gene amcB, recombinant enzyme expression in Escherichia coli Sterolibacterium denitrificans
gene kstD, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli strain XL10-Gold Sterolibacterium denitrificans
gene kstD1, recombinant enzyme expression in Escherichia coli strain BL21(DE3) Rhodococcus erythropolis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state kinetics, kinetic model Rhodococcus erythropolis
additional information
-
 additional information steady-state kinetics, kinetic model Sterolibacterium denitrificans
0.0237
-
 4-Cholesten-3-one pH 6.5, 30°C, recombinant enzyme Sterolibacterium denitrificans
0.0373
-
 2,6-dichlorophenol-indophenol pH 6.5, 30°C, recombinant enzyme, with 4-cholest-3-one Sterolibacterium denitrificans
0.2235
-
 2,6-dichlorophenol-indophenol pH 6.5, 30°C, recombinant enzyme, with 4-androstene-3,17-dione Sterolibacterium denitrificans
0.5292
-
 4-androstene-3,17-dione pH 6.5, 30°C, recombinant enzyme Sterolibacterium denitrificans

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane enzyme AcmB is located on the cytoplasmic side of the inner membranes of Sterolibacterium denitrificans Sterolibacterium denitrificans 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-androstene-3,17-dione + acceptor Rhodococcus erythropolis
-
 1,4-androstadiene-3,17-dione + reduced acceptor
-
 ?
4-androstene-3,17-dione + acceptor Sterolibacterium denitrificans
-
 1,4-androstadiene-3,17-dione + reduced acceptor
-
 ?
4-cholesten-3-one + 2,6-dichlorophenol-indophenol Sterolibacterium denitrificans
-
 ? + reduced acceptor
-
 ?

Organism

Organism UniProt Comment Textmining
Rhodococcus erythropolis Q9RA02
-
-
Sterolibacterium denitrificans A0A656Z7Q3
-
-
Sterolibacterium denitrificans A9XWD7
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli Sterolibacterium denitrificans
recombinant enzyme from Escherichia coli strain BL21(DE3) Rhodococcus erythropolis
recombinant enzyme from Escherichia coli strain XL10-Gold Sterolibacterium denitrificans

Reaction

Reaction Comment Organism Reaction ID
a 3-oxosteroid + acceptor = a 3-oxo-DELTA1-steroid + reduced acceptor ping-pong bi bi mechanism Sterolibacterium denitrificans
a
a 3-oxosteroid + acceptor = a 3-oxo-DELTA1-steroid + reduced acceptor sequential linear mechanism Rhodococcus erythropolis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-androstene-3,17-dione + acceptor
-
 Rhodococcus erythropolis 1,4-androstadiene-3,17-dione + reduced acceptor
-
 ?
4-androstene-3,17-dione + acceptor
-
 Sterolibacterium denitrificans 1,4-androstadiene-3,17-dione + reduced acceptor
-
 ?
4-androstene-3,17-dione + acceptor KSTD1, which is reported to be inactive with this substrates can catalyze the reaction if the solubility problem is addressed, e.g. by 2-hydroxpropyl-beta-cyclodextrin Rhodococcus erythropolis 1,4-androstadiene-3,17-dione + reduced acceptor
-
 ?
4-cholesten-3-one + 2,6-dichlorophenol-indophenol
-
 Rhodococcus erythropolis ? + reduced acceptor
-
 ?
4-cholesten-3-one + 2,6-dichlorophenol-indophenol
-
 Sterolibacterium denitrificans ? + reduced acceptor
-
 ?
6-dehydrotestosterone acetate + 2,6-dichlorophenol-indophenol
-
 Rhodococcus erythropolis ? + reduced 2,6-dichlorophenol-indophenol
-
 ?
6-dehydrotestosterone acetate + 2,6-dichlorophenol-indophenol
-
 Sterolibacterium denitrificans ? + reduced 2,6-dichlorophenol-indophenol
-
 ?
androstanolone + acceptor
-
 Rhodococcus erythropolis ? + reduced acceptor
-
 ?
androstanolone + acceptor
-
 Sterolibacterium denitrificans ? + reduced acceptor
-
 ?
diosgenone + acceptor
-
 Rhodococcus erythropolis ? + reduced acceptor
-
 ?
diosgenone + acceptor
-
 Sterolibacterium denitrificans ? + reduced acceptor
-
 ?
additional information enzyme substrate specificity, structure-function analysis. Conversion of 4-androstene-3,17-dione and cholest-4-en-3-one by isozyme AcmB2 proceeds at a similar rate. KSTDs catalyze regio- and stereoselective dehydrogenation between C1 and C2 atoms of steroid ring A. AcmB2 shows ability to catalyze DELTA1-dehydrogenation of steroids with the aliphatic side chain on the C17 position Sterolibacterium denitrificans ?
-
-
additional information enzyme substrate specificity, structure-function analysis. KSTDs catalyze regio- and stereoselective dehydrogenation between C1 and C2 atoms of steroid ring A. AcmB shows ability to catalyze DELTA1-dehydrogenation of steroids with the aliphatic side chain on the C17 position. AcmB indeed exhibits a significantly higher affinity to cholest-4-en-3-one than to 4-androstene-3,17-dione Sterolibacterium denitrificans ?
-
-
additional information enzyme substrate specificity, structure-function analysis. KSTDs catalyze regio- and stereoselective dehydrogenation between C1 and C2 atoms of steroid ring A. Enzyme KSTD1 prefers smaller 3-oxosteroids Rhodococcus erythropolis ?
-
-
progesterone + 2,6-dichlorophenol-indophenol
-
 Rhodococcus erythropolis pregna-1,4-diene-3,20-dione + reduced 2,6-dichlorophenol-indophenol
-
 ?
progesterone + 2,6-dichlorophenol-indophenol
-
 Sterolibacterium denitrificans pregna-1,4-diene-3,20-dione + reduced 2,6-dichlorophenol-indophenol
-
 ?
testosterone propionate + 2,6-dichlorophenol-indophenol
-
 Rhodococcus erythropolis 17beta-hydroxyandrost-1,4-diene-3-one propionate + reduced 2,6-dichlorophenol-indophenol
-
 ?
testosterone propionate + 2,6-dichlorophenol-indophenol
-
 Sterolibacterium denitrificans 17beta-hydroxyandrost-1,4-diene-3-one propionate + reduced 2,6-dichlorophenol-indophenol
-
 ?

Synonyms

Synonyms Comment Organism
3-ketosteroid delta1-dehydrogenase
-
 Rhodococcus erythropolis
3-ketosteroid delta1-dehydrogenase
-
 Sterolibacterium denitrificans
AcmB
-
 Sterolibacterium denitrificans
AcmB2
-
 Sterolibacterium denitrificans
cholest-4-en-3-one DELTA1-dehydrogenase
-
 Sterolibacterium denitrificans
DELTA1-KstD
-
 Rhodococcus erythropolis
DELTA1-KstD
-
 Sterolibacterium denitrificans
KstD
-
 Sterolibacterium denitrificans
KSTD1
-
 Rhodococcus erythropolis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
-
 Rhodococcus erythropolis
30
-
-
 Sterolibacterium denitrificans
30
-
 assay at Sterolibacterium denitrificans

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.8
-
 4-Cholesten-3-one pH 6.5, 30°C, recombinant enzyme Sterolibacterium denitrificans
46.1
-
 4-androstene-3,17-dione pH 6.5, 30°C, recombinant enzyme Sterolibacterium denitrificans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
-
 Sterolibacterium denitrificans
6.5
-
 assay at Sterolibacterium denitrificans
8
-
-
 Rhodococcus erythropolis

Cofactor

Cofactor Comment Organism Structure
2,6-dichlorophenolindophenol DCPIP Rhodococcus erythropolis
2,6-dichlorophenolindophenol DCPIP Sterolibacterium denitrificans

General Information

General Information Comment Organism
evolution 3-oxosteroid DELTA1-dehydrogenases are found in a large variety of microorganisms, especially in bacteria belonging to the phylum Actinobacteria Rhodococcus erythropolis
evolution 3-oxosteroid DELTA1-dehydrogenases are found in a large variety of microorganisms, especially in bacteria belonging to the phylum Actinobacteria Sterolibacterium denitrificans
additional information three-dimensional structure of a 3-oxosteroid DELTA1-dehydrogenase and structure-function analysis, enzyme reaction mechanism analysis, overview Sterolibacterium denitrificans
additional information three-dimensional structure of a 3-oxosteroid DELTA1-dehydrogenase and structure-function analysis, enzyme reaction mechanism analysis, overview. Molecular dynamics simulations on KSTD1 from Rhodococcus erythropolis Rhodococcus erythropolis
physiological function 3-oxosteroid DELTA1-dehydrogenases (DELTA1-KSTDs) are FAD-dependent enzymes that catalyze the introduction of a double bond between the C1 and C2 atoms of the A-ring of 3-ketosteroid substrates. They play a critical role in the early steps of the degradation of the steroid core. Enzyme DELTA1-KSTD is also essential for steroid ring opening under anaerobic conditions Rhodococcus erythropolis
physiological function 3-oxosteroid DELTA1-dehydrogenases (DELTA1-KSTDs) are FAD-dependent enzymes that catalyze the introduction of a double bond between the C1 and C2 atoms of the A-ring of 3-ketosteroid substrates. They play a critical role in the early steps of the degradation of the steroid core. Enzyme DELTA1-KSTD is also essential for steroid ring opening under anaerobic conditions Sterolibacterium denitrificans

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
87.1
-
 4-androstene-3,17-dione pH 6.5, 30°C, recombinant enzyme Sterolibacterium denitrificans