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Information on EC 6.2.1.42 - 3-oxocholest-4-en-26-oate-CoA ligase
for references in articles please use BRENDA:EC6.2.1.42
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EC Tree 6 Ligases
6.2 Forming carbon-sulfur bonds
6.2.1 Acid-thiol ligases
6.2.1.42 3-oxocholest-4-en-26-oate-CoA ligase
IUBMB Comments
The enzyme, characterized from actinobacterium Mycobacterium tuberculosis, catalyses a step in the degradation of cholesterol. It is responsible for the activation of the C8 side chain. 3β-hydroxycholest-5-en-26-oate can also be used as substrate.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
fadd19, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
fadD19
FadD19-2
FadD19-4
steroid-CoA ligase
fadD19
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + (25S)-3-oxocholest-4-en-26-oate + CoA = AMP + diphosphate + (25S)-3-oxocholest-4-en-26-oyl-CoA
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
cholesterol degradation to androstenedione I (cholesterol oxidase), cholesterol degradation to androstenedione II (cholesterol dehydrogenase), cholesterol degradation to androstenedione III (anaerobic)
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SYSTEMATIC NAME
IUBMB Comments
3-oxocholest-4-en-26-oate:CoA ligase (AMP-forming)
The enzyme, characterized from actinobacterium Mycobacterium tuberculosis, catalyses a step in the degradation of cholesterol. It is responsible for the activation of the C8 side chain. 3beta-hydroxycholest-5-en-26-oate can also be used as substrate.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + (25S)-3-oxocholest-4-en-26-oate + CoA
AMP + diphosphate + (25S)-3-oxocholest-4-en-26-oyl-CoA
ATP + (25S)-3-oxocholest-4-en-26-oate + CoA
AMP + diphosphate + (25S)-3-oxocholest-4-en-26-oyl-CoA
Substrates: -
Products: -
Products: -
?
ATP + (25S)-3-oxocholest-4-en-26-oate + CoA
AMP + diphosphate + (25S)-3-oxocholest-4-en-26-oyl-CoA
Substrates: -
Products: -
Products: -
?
ATP + 3-hydroxy-5-cholesten-26-oate
?
-
Substrates: -
Products: -
Products: -
?
ATP + 3-hydroxy-5-cholesten-26-oate
?
-
Substrates: -
Products: -
Products: -
?
ATP + 3-oxocholest-4-en-26-oate + CoA
AMP + diphosphate + 3-oxocholest-4-en-26-oyl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + 3-oxocholest-4-en-26-oate + CoA
AMP + diphosphate + 3-oxocholest-4-en-26-oyl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + 3-oxocholest-4-en-26-oate + CoA
AMP + diphosphate + 3-oxocholest-4-en-26-oyl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + 3-oxocholest-4-en-26-oate + CoA
AMP + diphosphate + 3-oxocholest-4-en-26-oyl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + 3beta-hydroxy-5-cholesten-26-oate + CoA
?
Substrates: the enzyme only shows activity with compound that have a C8 side chain
Products: -
Products: -
?
ATP + 3beta-hydroxy-5-cholesten-26-oate + CoA
?
Substrates: the enzyme only shows activity with compound that have a C8 side chain
Products: -
Products: -
?
ATP + 5-cholenic acid-3beta-ol
?
-
Substrates: -
Products: -
Products: -
?
ATP + 5-cholestene-26-oic acid-3beta-ol
?
-
Substrates: -
Products: -
Products: -
?
ATP + 5-cholestene-26-oic acid-3beta-ol
?
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with cholate, chenodeoxycholate, 3-oxo-23,24-bisnorchol-4-en-22-oic acid, 3-hydroxy-9-oxo-9,10-seco-23,24-bisnorchola-1,3,5(10)-trien-22-oate, 1beta(2'-propanoate)-3aalpha-H-4alpha(3'-propanoate)-7abeta-methylhexahydro-5-indanone, and 3aalpha-H-4alpha(3'-propanoate)-7abeta-methylhexahydro-1,5-indanedione
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with cholate, chenodeoxycholate, 3-oxo-23,24-bisnorchol-4-en-22-oic acid, 3-hydroxy-9-oxo-9,10-seco-23,24-bisnorchola-1,3,5(10)-trien-22-oate, 1beta(2'-propanoate)-3aalpha-H-4alpha(3'-propanoate)-7abeta-methylhexahydro-5-indanone, and 3aalpha-H-4alpha(3'-propanoate)-7abeta-methylhexahydro-1,5-indanedione
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + (25S)-3-oxocholest-4-en-26-oate + CoA
AMP + diphosphate + (25S)-3-oxocholest-4-en-26-oyl-CoA
ATP + (25S)-3-oxocholest-4-en-26-oate + CoA
AMP + diphosphate + (25S)-3-oxocholest-4-en-26-oyl-CoA
Substrates: -
Products: -
Products: -
?
ATP + (25S)-3-oxocholest-4-en-26-oate + CoA
AMP + diphosphate + (25S)-3-oxocholest-4-en-26-oyl-CoA
Substrates: -
Products: -
Products: -
?
ATP + 3-oxocholest-4-en-26-oate + CoA
AMP + diphosphate + 3-oxocholest-4-en-26-oyl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + 3-oxocholest-4-en-26-oate + CoA
AMP + diphosphate + 3-oxocholest-4-en-26-oyl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + 3-oxocholest-4-en-26-oate + CoA
AMP + diphosphate + 3-oxocholest-4-en-26-oyl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + 3-oxocholest-4-en-26-oate + CoA
AMP + diphosphate + 3-oxocholest-4-en-26-oyl-CoA
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5'-O-(lithocholoyl sulfamoyl) adenosine
-
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
Actinobacterial acyl coenzyme A synthetases involved in steroid side-chain catabolism.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00688
3beta-hydroxy-5-cholesten-26-oate
pH 7.5, 37°C
0.02223
3beta-hydroxy-5-cholesten-26-oate
pH 7.5, 37°C
0.0321
3beta-hydroxy-5-cholesten-26-oate
pH 7.5, 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.05
3beta-hydroxy-5-cholesten-26-oate
pH 7.5, 37°C
7.61
3beta-hydroxy-5-cholesten-26-oate
pH 7.5, 37°C
12.34
3beta-hydroxy-5-cholesten-26-oate
pH 7.5, 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
126.17
3beta-hydroxy-5-cholesten-26-oate
pH 7.5, 37°C
342.33
3beta-hydroxy-5-cholesten-26-oate
pH 7.5, 37°C
1793.6
3beta-hydroxy-5-cholesten-26-oate
pH 7.5, 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.003217
5'-O-(lithocholoyl sulfamoyl) adenosine
pH 7.5, 37°C
-
0.005983
5'-O-(lithocholoyl sulfamoyl) adenosine
pH 7.5, 37°C
-
0.007735
5'-O-(lithocholoyl sulfamoyl) adenosine
pH 7.5, 37°C
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.06354
5'-O-(lithocholoyl sulfamoyl) adenosine
Mycolicibacterium smegmatis
pH 7.5, 37°C
-
0.06556
5'-O-(lithocholoyl sulfamoyl) adenosine
Mycolicibacterium smegmatis
pH 7.5, 37°C
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
deletion of fadD19 completely blocks side chain degradation of C-24 branched sterols but not that of cholesterol
malfunction
-
deletion of fadD19 completely blocks side chain degradation of C-24 branched sterols but not that of cholesterol
-
metabolism
-
the enzyme essential for degradation of C-24 branched sterol side chains
metabolism
the enzyme plays an essential role in C-24 branched side chain sterol degradation, overview
metabolism
the enzyme is involved in mycobacterial steroid side-chain catabolism
metabolism
-
the enzyme essential for degradation of C-24 branched sterol side chains
-
metabolism
-
the enzyme is involved in mycobacterial steroid side-chain catabolism
-
metabolism
-
the enzyme plays an essential role in C-24 branched side chain sterol degradation, overview
-
physiological function
the enzyme encoded by gene fadD19 plays a role in the degradation process of the side chain of cholesterol and beta-sitosterol, but is not essential for viability. FadD19 is required in the initial step of the biodegradation of C-24 branched sterol side chains in Mycobacterium smegmatis mc2155, like beta-sitosterol, but not those carrying a straight chain, like cholesterol. The enzyme has an essential role of FadD19 in the early step of beta-sitosterol degradation
physiological function
-
the enzyme encoded by gene fadD19 plays a role in the degradation process of the side chain of cholesterol and beta-sitosterol, but is not essential for viability. FadD19 is required in the initial step of the biodegradation of C-24 branched sterol side chains in Mycobacterium smegmatis mc2155, like beta-sitosterol, but not those carrying a straight chain, like cholesterol. The enzyme has an essential role of FadD19 in the early step of beta-sitosterol degradation
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). FAC19_MYCS2
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
551
0
60246
Swiss-Prot
other Location (Reliability: 1)
FAC19_MYCMM
Mycobacterium marinum (strain ATCC BAA-535 / M)
550
0
59946
Swiss-Prot
-
FAC19_RHORH
555
0
60602
Swiss-Prot
other Location (Reliability: 5)
FAC19_MYCTO
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
548
0
59741
Swiss-Prot
other Location (Reliability: 1)
FAC19_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
548
0
59741
Swiss-Prot
-
FAC19_MYCBO
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
548
0
59741
Swiss-Prot
-
A0A0E9AQ95_MYCTX
548
0
59767
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0H3M9B4_MYCBP
Mycobacterium bovis (strain BCG / Pasteur 1173P2)
548
0
59741
TrEMBL
Secretory Pathway (Reliability: 2)
A0A679LLR8_MYCBO
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
548
0
59741
TrEMBL
-
A0A9P2M1Y3_MYCTX
548
0
59741
TrEMBL
-
A0AAU0Q5R5_9MYCO
548
0
59741
TrEMBL
other Location (Reliability: 1)
A0AB72XQR6_MYCCP
Mycobacterium canettii (strain CIPT 140010059)
548
0
59739
TrEMBL
-
A0AB74LLT7_MYCBI
548
0
59741
TrEMBL
Mitochondrion (Reliability: 5)
A5U8I9_MYCTA
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
548
0
59741
TrEMBL
-
R4MM20_MYCTX
548
0
59741
TrEMBL
-
A0QUK6_MYCS2
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
550
0
58967
TrEMBL
-
A0QYK2_MYCS2
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
551
0
59235
TrEMBL
-
I7FZL8_MYCS2
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
542
0
58776
TrEMBL
other Location (Reliability: 5)
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of complemented mutant carrying an intact fadD19 under control of its natural putative promoter (Mycobacterium smegmatis DELTAfadD19; attB::PfadD19fadD19). The complemented strain, but not the DELTAfadD19 mutant, is able to degrade beta-sitosterol with kinetics similar to that of wild-type
additional information
-
construction of complemented mutant carrying an intact fadD19 under control of its natural putative promoter (Mycobacterium smegmatis DELTAfadD19; attB::PfadD19fadD19). The complemented strain, but not the DELTAfadD19 mutant, is able to degrade beta-sitosterol with kinetics similar to that of wild-type
additional information
-
construction of complemented mutant carrying an intact fadD19 under control of its natural putative promoter (Mycobacterium smegmatis DELTAfadD19; attB::PfadD19fadD19). The complemented strain, but not the DELTAfadD19 mutant, is able to degrade beta-sitosterol with kinetics similar to that of wild-type
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene fadD19, DNA and amino acid sequence determination and analysis, chromosomal localization, expression analysis
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wilbrink, M.H.; Petrusma, M.; Dijkhuizen, L.; van der Geize, R.
FadD19 of Rhodococcus rhodochrous DSM43269, a steroid-coenzyme A ligase essential for degradation of C-24 branched sterol side chains
Appl. Environ. Microbiol.
77
4455-4464
2011
Rhodococcus rhodochrous, Rhodococcus rhodochrous DSM 43269
brenda
Casabon, I.; Swain, K.; Crowe, A.M.; Eltis, L.D.; Mohn, W.W.
Actinobacterial acyl coenzyme A synthetases involved in steroid side-chain catabolism
J. Bacteriol.
196
579-587
2014
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Wronska, N.; Brzostek, A.; Szewczyk, R.; Sobon, A.; Dziadek, J.; Lisowska, K.
The role of fadD19 and echA19 in sterol side chain degradation by mycobacterium smegmatis
Molecules
21
598-611
2016
Mycolicibacterium smegmatis (I7FZL8), Mycolicibacterium smegmatis, Mycolicibacterium smegmatis mc2155 (I7FZL8)
brenda
Niu, Y.; Ge, F.; Yang, Y.; Ren, Y.; Li, W.; Chen, G.; Wen, D.; Liu, F.; Xiong, L.
Biochemical characterization of acyl-coenzyme A synthetases involved in mycobacterial steroid side-chain catabolism and molecular design synthesis of an anti-mycobacterial agent
3 Biotech
9
169
2019
Mycolicibacterium smegmatis (A0R4Q2), Mycolicibacterium smegmatis (A0QUK6), Mycolicibacterium smegmatis (A0QYK2), Mycolicibacterium smegmatis ATCC 700084 (A0R4Q2), Mycolicibacterium smegmatis ATCC 700084 (A0QUK6), Mycolicibacterium smegmatis ATCC 700084 (A0QYK2)
brenda
EXTERNAL LINKS (specific for EC-Number 6.2.1.42)
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