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Information on EC 6.2.1.3 - long-chain-fatty-acid-CoA ligase and Organism(s) Pseudomonas aeruginosa

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EC Tree
     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.3 long-chain-fatty-acid-CoA ligase
IUBMB Comments
Acts on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. The liver enzyme acts on acids from C6 to C20; that from brain shows high activity up to C24.
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This record set is specific for:
Pseudomonas aeruginosa
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
Synonyms
acsl1, fatp4, fatty acid transport protein, acsl3, acsl5, long-chain acyl-coa synthetase, fatty acyl-coa synthetase, acsl6, fatp2, acyl-coa synthetase long-chain, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACS3
-
-
-
-
Acyl coenzyme A synthetase
-
-
-
-
Acyl-activating enzyme
-
-
-
-
Acyl-CoA ligase
-
-
-
-
Acyl-CoA synthetase
Acyl-CoA synthetase 3
-
-
-
-
Acyl-coenzyme A ligase
-
-
-
-
FAA1
-
-
-
-
Fatty acid CoA ligase
-
-
-
-
Fatty acid thiokinase (long chain)
-
-
-
-
Fatty acyl-coenzyme A synthetase
-
-
-
-
Fatty-acyl-CoA ligase
-
-
-
-
LACS
-
-
-
-
LCFA synthetase
-
-
-
-
Long chain fatty acyl CoA ligase
-
-
-
-
Long chain fatty acyl-CoA synthetase
-
-
-
-
Long-chain acyl CoA synthetase
-
-
-
-
Long-chain acyl-CoA synthetase I
-
-
-
-
Long-chain acyl-CoA synthetase II
-
-
-
-
Long-chain acyl-coenzyme A synthetase
-
-
-
-
Long-chain fatty acyl coenzyme A synthetase
-
-
-
-
mACS4
-
-
-
-
Oleoyl-CoA synthetase
-
-
-
-
Palmitoyl coenzyme A synthetase
-
-
-
-
Palmitoyl-CoA ligase
-
-
-
-
Palmityl-coenzyme A synthetase
-
-
-
-
Pristanoyl-CoA synthetase
-
-
-
-
Stearoyl-CoA synthetase
-
-
-
-
Thiokinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
-
-
-
-
Phosphorylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
long-chain fatty acid:CoA ligase (AMP-forming)
Acts on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. The liver enzyme acts on acids from C6 to C20; that from brain shows high activity up to C24.
CAS REGISTRY NUMBER
COMMENTARY hide
9013-18-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + linoleate + CoA
AMP + diphosphate + linoleoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + oleate + CoA
AMP + diphosphate + oleoyl-CoA
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Triacsin A
-
non-competitive with respect to ATP and coenzyme A
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.93
coenzyme A
-
oleate activation
0.041
linoleate
-
ATP, , oleate activation
0.101
oleic acid
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
when compared to the wild-type strain, the fadD2 mutant exhibits decreased production of lipase, protease, rhamnolipid and phospholipase, and retardation of both swimming and swarming motilities. Interestingly, fadD1 mutant shows only increased swarming motility. Growth analysis of the fadD mutants show noticeable deficiencies in utilizing fatty acids and phosphatidylcholine as the sole carbon source, altered swimming and swarming motility of fadD mutants
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A0C7AJY2_PSEAI
608
0
67620
TrEMBL
-
A0A8G6G9P7_PSEAI
562
0
61721
TrEMBL
-
A0A6A9JYJ0_PSEAI
562
0
61738
TrEMBL
-
A0A485FLT3_PSEAI
551
0
60403
TrEMBL
-
A0A485EQF0_PSEAI
555
0
61317
TrEMBL
-
A0A8G3P5U8_PSEAI
562
0
61779
TrEMBL
-
A0A5E5QT93_PSEAI
549
0
59506
TrEMBL
-
A0A8G4MA60_PSEAI
562
0
61737
TrEMBL
-
A0A8G3CH61_PSEAI
562
0
61750
TrEMBL
-
A0A4P0TBA9_PSEAI
595
1
63040
TrEMBL
-
A0A485EH61_PSEAI
326
0
35847
TrEMBL
-
A0A8G3AAA9_PSEAI
562
0
61751
TrEMBL
-
A0A0A8RC61_PSEAI
562
0
61641
TrEMBL
-
A0A8G7MB68_PSEAI
562
0
61777
TrEMBL
-
A0A8F9NV63_PSEAI
608
0
67620
TrEMBL
-
A0A8G3I9A8_PSEAI
562
0
61751
TrEMBL
-
A0A7M3AY87_PSEAI
562
0
61723
TrEMBL
-
A0A8G4DYL9_PSEAI
562
0
61691
TrEMBL
-
A0A8B4ZFD3_PSEAI
562
0
61721
TrEMBL
-
A0A485F5C5_PSEAI
562
0
61655
TrEMBL
-
A0A8G7PL27_PSEAI
562
0
61751
TrEMBL
-
A0A4P0UB85_PSEAI
334
0
36990
TrEMBL
-
A0A3E1N1M9_PSEAI
562
0
61751
TrEMBL
-
A0A8G3K731_PSEAI
562
0
61707
TrEMBL
-
A0A0D6GUX0_PSEAI
562
0
61737
TrEMBL
-
A0A6M3V7I9_PSEAI
562
0
61751
TrEMBL
-
A0A2R3ISC2_PSEAI
555
0
61458
TrEMBL
-
A0A8G7TKU5_PSEAI
562
0
61707
TrEMBL
-
A0A8G3M5Y7_PSEAI
562
0
61791
TrEMBL
-
A0A509JNW8_PSEAI
562
0
61779
TrEMBL
-
A0A8F9KCD8_PSEAI
608
0
67650
TrEMBL
-
A0A2R4KR40_PSEAI
560
0
62344
TrEMBL
-
A0A080VPF0_PSEAI
562
0
61723
TrEMBL
-
A0A485FJG6_PSEAI
560
0
62303
TrEMBL
-
A0A8G7SDV8_PSEAI
562
0
61779
TrEMBL
-
A0A643EMC9_PSEAI
562
0
61736
TrEMBL
-
A0A4P0VE31_PSEAI
441
0
48075
TrEMBL
-
A0A485IUE6_PSEAI
561
0
62392
TrEMBL
-
A0A4P0UCH1_PSEAI
218
0
23701
TrEMBL
-
A0A485EYS7_PSEAI
534
0
59164
TrEMBL
-
A0A0C7D2K4_PSEAI
560
0
62316
TrEMBL
-
A0A2R3IMU0_PSEAI
562
0
61736
TrEMBL
-
A0A8G6Y0W0_PSEAI
562
0
61751
TrEMBL
-
A0A8G4B4G8_PSEAI
562
0
61748
TrEMBL
-
A0A2R4KQE1_PSEAI
632
0
69015
TrEMBL
-
A0A2C9WXX7_PSEAI
562
0
61685
TrEMBL
-
A0A8F9JSP6_PSEAI
608
0
67669
TrEMBL
-
A0A8G6A6X9_PSEAI
562
0
61746
TrEMBL
-
A0A8G2VWB7_PSEAI
562
0
61772
TrEMBL
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene fadD1, DNA and amino acid sequence determination, genetic organization, complemention of Escherichia coli strain fadD-/fadR- strain E2011. SMART mapping of the transcriptional start site for fadD1
gene fadD2, DNA and amino acid sequence determination, genetic organization, complemention of Escherichia coli strain fadD-/fadR- strain E2011. SMART mapping of the transcriptional start site fadD1
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tomoda, H.; Igarashi, K.; Omura, S.
Inhibition of acyl-CoA synthetase by triacsins
Biochim. Biophys. Acta
921
595-598
1987
Pseudomonas aeruginosa, Rattus norvegicus
Manually annotated by BRENDA team
Kang, Y.; Zarzycki-Siek, J.; Walton, C.B.; Norris, M.H.; Hoang, T.T.
Multiple FadD acyl-CoA synthetases contribute to differential fatty acid degradation and virulence in Pseudomonas aeruginosa
PLoS ONE
5
e13557
2010
Pseudomonas aeruginosa (Q9HYU3), Pseudomonas aeruginosa (Q9HYU4), Pseudomonas aeruginosa
Manually annotated by BRENDA team