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Information on EC 6.2.1.57 - long-chain fatty acid adenylase/transferase FadD23
for references in articles please use BRENDA:EC6.2.1.57
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EC Tree 6 Ligases
6.2 Forming carbon-sulfur bonds
6.2.1 Acid-thiol ligases
6.2.1.57 long-chain fatty acid adenylase/transferase FadD23
IUBMB Comments
This mycobacterial enzyme activates palmitate and stearate by adenylation, followed by their loading onto the polyketide synthase EC 2.3.1.287, phthioceranic/hydroxyphthioceranic acid synthase.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 6.2.1.57
-
mycobacterial
- tuberculosis
- faals
- adenylate
- envelope
- polyketide
-
mycolic
-
fadd32
- ligases
-
lipopeptide
-
non-ribosomal
-
meromycolic
-
acyl-adenylate
- phthiocerol
-
dimycocerosates
-
antituberculous
-
adenylate-forming
-
starter
-
glycopeptidolipids
- acyl-acp
- smegmatis
-
pdims
- marinum
Reaction Schemes
show+
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=
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+
a holo-[(hydroxy)phthioceranic acid synthase]
=
+
+
a stearoyl-[(hydroxy)phthioceranic acid synthase]
+
+
=
+
+
+
+
a holo-[(hydroxy)phthioceranic acid synthase]
=
+
+
a palmitoyl-[(hydroxy)phthioceranic acid synthase]
Synonyms
fatty acyl-amp ligase, fadd23, rv3826, fatty-acyl amp ligase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FAAL
FAAL23
fadD23
fatty acyl AMP ligase
fatty acyl-AMP ligase
fatty-acyl AMP ligase
long-chain fatty acid adenylyltransferase FadD23
-
-
-
-
long-chain-fatty-acid-AMP ligase FadD23
Rv3826
fadD23
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(palmitoyl)adenylate + a holo-[(hydroxy)phthioceranic acid synthase] = AMP + a palmitoyl-[(hydroxy)phthioceranic acid synthase]
(2b)
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-
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(stearoyl)adenylate + a holo-[(hydroxy)phthioceranic acid synthase] = AMP + a stearoyl-[(hydroxy)phthioceranic acid synthase]
(1b)
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-
-
ATP + palmitate + a holo-[(hydroxy)phthioceranic acid synthase] = AMP + diphosphate + a palmitoyl-[(hydroxy)phthioceranic acid synthase]
overall reaction
-
-
-
ATP + palmitate = diphosphate + (palmitoyl)adenylate
(2a)
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-
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ATP + stearate + a holo-[(hydroxy)phthioceranic acid synthase] = AMP + diphosphate + a stearoyl-[(hydroxy)phthioceranic acid synthase]
overall reaction
-
-
-
ATP + stearate = diphosphate + (stearoyl)adenylate
(1a)
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-
-
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SYSTEMATIC NAME
IUBMB Comments
palmitate:holo-[(hydroxy)phthioceranic acid synthase] ligase
This mycobacterial enzyme activates palmitate and stearate by adenylation, followed by their loading onto the polyketide synthase EC 2.3.1.287, phthioceranic/hydroxyphthioceranic acid synthase.
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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 + laurate + a holo-[(hydroxy)phthioceranic acid synthase]
AMP + diphosphate + lauroyl-[(hydroxy)phthioceranic acid synthase]
ATP + palmitate + a holo-[(hydroxy)phthioceranic acid synthase]
AMP + diphosphate + a palmitoyl-[(hydroxy)phthioceranic acid synthase]
ATP + palmitate + holo-[(hydroxy)phthioceranic acid synthase]
AMP + diphosphate + palmitoyl-[(hydroxy)phthioceranic acid synthase]
ATP + laurate + a holo-[(hydroxy)phthioceranic acid synthase]
AMP + diphosphate + lauroyl-[(hydroxy)phthioceranic acid synthase]
Substrates: overall reaction
Products: -
Products: -
?
ATP + laurate + a holo-[(hydroxy)phthioceranic acid synthase]
AMP + diphosphate + lauroyl-[(hydroxy)phthioceranic acid synthase]
Substrates: overall reaction
Products: -
Products: -
?
ATP + laurate + a holo-[(hydroxy)phthioceranic acid synthase]
AMP + diphosphate + lauroyl-[(hydroxy)phthioceranic acid synthase]
Substrates: overall reaction
Products: -
Products: -
?
ATP + palmitate + a holo-[(hydroxy)phthioceranic acid synthase]
AMP + diphosphate + a palmitoyl-[(hydroxy)phthioceranic acid synthase]
Substrates: overall reaction
Products: -
Products: -
?
ATP + palmitate + a holo-[(hydroxy)phthioceranic acid synthase]
AMP + diphosphate + a palmitoyl-[(hydroxy)phthioceranic acid synthase]
Substrates: overall reaction
Products: -
Products: -
?
ATP + palmitate + a holo-[(hydroxy)phthioceranic acid synthase]
AMP + diphosphate + a palmitoyl-[(hydroxy)phthioceranic acid synthase]
Substrates: overall reaction
Products: -
Products: -
?
ATP + palmitate + holo-[(hydroxy)phthioceranic acid synthase]
AMP + diphosphate + palmitoyl-[(hydroxy)phthioceranic acid synthase]
Substrates: overall reaction
Products: -
Products: -
?
ATP + palmitate + holo-[(hydroxy)phthioceranic acid synthase]
AMP + diphosphate + palmitoyl-[(hydroxy)phthioceranic acid synthase]
Substrates: overall reaction
Products: -
Products: -
?
ATP + palmitate + holo-[(hydroxy)phthioceranic acid synthase]
AMP + diphosphate + palmitoyl-[(hydroxy)phthioceranic acid synthase]
Substrates: overall reaction
Products: -
Products: -
?
additional information
?
-
Substrates: evaluation of long-chain saturated fatty acids as biological substrates of FadD23 through structural, biological, and chemical analyses. The FadD23 N-terminal domain alone cannot bind palmitic acid without C-terminal domain facilitation since it is almost inactive after removing the C-terminal domain. No activity with stearate and octanoate
Products: -
Products: -
-
additional information
?
-
Substrates: evaluation of long-chain saturated fatty acids as biological substrates of FadD23 through structural, biological, and chemical analyses. The FadD23 N-terminal domain alone cannot bind palmitic acid without C-terminal domain facilitation since it is almost inactive after removing the C-terminal domain. No activity with stearate and octanoate
Products: -
Products: -
-
additional information
?
-
Substrates: evaluation of long-chain saturated fatty acids as biological substrates of FadD23 through structural, biological, and chemical analyses. The FadD23 N-terminal domain alone cannot bind palmitic acid without C-terminal domain facilitation since it is almost inactive after removing the C-terminal domain. No activity with stearate and octanoate
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 + laurate + a holo-[(hydroxy)phthioceranic acid synthase]
AMP + diphosphate + lauroyl-[(hydroxy)phthioceranic acid synthase]
ATP + palmitate + a holo-[(hydroxy)phthioceranic acid synthase]
AMP + diphosphate + a palmitoyl-[(hydroxy)phthioceranic acid synthase]
ATP + laurate + a holo-[(hydroxy)phthioceranic acid synthase]
AMP + diphosphate + lauroyl-[(hydroxy)phthioceranic acid synthase]
Substrates: overall reaction
Products: -
Products: -
?
ATP + laurate + a holo-[(hydroxy)phthioceranic acid synthase]
AMP + diphosphate + lauroyl-[(hydroxy)phthioceranic acid synthase]
Substrates: overall reaction
Products: -
Products: -
?
ATP + laurate + a holo-[(hydroxy)phthioceranic acid synthase]
AMP + diphosphate + lauroyl-[(hydroxy)phthioceranic acid synthase]
Substrates: overall reaction
Products: -
Products: -
?
ATP + palmitate + a holo-[(hydroxy)phthioceranic acid synthase]
AMP + diphosphate + a palmitoyl-[(hydroxy)phthioceranic acid synthase]
Substrates: overall reaction
Products: -
Products: -
?
ATP + palmitate + a holo-[(hydroxy)phthioceranic acid synthase]
AMP + diphosphate + a palmitoyl-[(hydroxy)phthioceranic acid synthase]
Substrates: overall reaction
Products: -
Products: -
?
ATP + palmitate + a holo-[(hydroxy)phthioceranic acid synthase]
AMP + diphosphate + a palmitoyl-[(hydroxy)phthioceranic acid synthase]
Substrates: overall reaction
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Clonal Diversification and Changes in Lipid Traits and Colony Morphology in Mycobacterium abscessus Clinical Isolates.
Tuberculosis
Assay Development for Identifying Inhibitors of the Mycobacterial FadD32 Activity.
Tuberculosis
Crystallization and preliminary X-ray crystallographic studies of the N-terminal domain of FadD28, a fatty-acyl AMP ligase from Mycobacterium tuberculosis.
Tuberculosis
Molecular basis of the functional divergence of fatty acyl-AMP ligase biosynthetic enzymes of Mycobacterium tuberculosis.
Tuberculosis
Selection of transposon mutants of Mycobacterium tuberculosis with increased macrophage infectivity identifies fadD23 to be involved in sulfolipid production and association with macrophages.
Tuberculosis
Structural and functional studies of fatty acyl adenylate ligases from E. coli and L. pneumophila.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
evolution
malfunction
metabolism
physiological function
additional information
evolution
FadD23 is one of the 34 fatty acid adenylating enzymes (FadDs) in Mycobacterium tuberculosis, FAD enzyme structure comparisons, overview
evolution
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FadD23 is one of the 34 fatty acid adenylating enzymes (FadDs) in Mycobacterium tuberculosis, FAD enzyme structure comparisons, overview
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evolution
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FadD23 is one of the 34 fatty acid adenylating enzymes (FadDs) in Mycobacterium tuberculosis, FAD enzyme structure comparisons, overview
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malfunction
-
enzyme gene disruption leads to deficiency in the production of cell wall sulfolipids
malfunction
mutation at the active site of FadD23 greatly influences enzymatic activity. The FadD23 N-terminal domain alone cannot bind palmitic acid without C-terminal domain facilitation since it is almost inactive after removing the C-terminal domain
malfunction
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enzyme gene disruption leads to deficiency in the production of cell wall sulfolipids
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malfunction
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mutation at the active site of FadD23 greatly influences enzymatic activity. The FadD23 N-terminal domain alone cannot bind palmitic acid without C-terminal domain facilitation since it is almost inactive after removing the C-terminal domain
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malfunction
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mutation at the active site of FadD23 greatly influences enzymatic activity. The FadD23 N-terminal domain alone cannot bind palmitic acid without C-terminal domain facilitation since it is almost inactive after removing the C-terminal domain
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metabolism
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the enzyme is involved in activation of fatty acids for synthesis of complex lipids like glycopeptidolipid
metabolism
FadD23-Pks2 plays a central role in the SL-1 synthesis pathway. Sulfolipid-1 consists of one trehalose-2-sulfate (T2S) disaccharide with four acyl groups. An acyltransferase, PapA2, adds one straight-chain fatty acid to the 2'-position of T2S to generate SL659, another acyltransferase, PapA1, transfers one multiple methyl-branched (hydroxy) phthioceranoic acid to the 3'-position of SL659 to form SL1278, additional catalytic steps are acylation at the 6- and 6'-positions of SL1278 with two multiple methyl-branched (hydroxy) phthioceranoic acids, most likely through membrane-associated Chp1 to produce fully elaborated SL-1. These multiple methyl-branched (hydroxy) phthioceranoic acids are synthesized by polyketide synthase 2 (Pks2) using an activated fatty acid starter unit provided by fatty acyl AMP ligase FadD23 (FAAL23)
metabolism
-
FadD23-Pks2 plays a central role in the SL-1 synthesis pathway. Sulfolipid-1 consists of one trehalose-2-sulfate (T2S) disaccharide with four acyl groups. An acyltransferase, PapA2, adds one straight-chain fatty acid to the 2'-position of T2S to generate SL659, another acyltransferase, PapA1, transfers one multiple methyl-branched (hydroxy) phthioceranoic acid to the 3'-position of SL659 to form SL1278, additional catalytic steps are acylation at the 6- and 6'-positions of SL1278 with two multiple methyl-branched (hydroxy) phthioceranoic acids, most likely through membrane-associated Chp1 to produce fully elaborated SL-1. These multiple methyl-branched (hydroxy) phthioceranoic acids are synthesized by polyketide synthase 2 (Pks2) using an activated fatty acid starter unit provided by fatty acyl AMP ligase FadD23 (FAAL23)
-
metabolism
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FadD23-Pks2 plays a central role in the SL-1 synthesis pathway. Sulfolipid-1 consists of one trehalose-2-sulfate (T2S) disaccharide with four acyl groups. An acyltransferase, PapA2, adds one straight-chain fatty acid to the 2'-position of T2S to generate SL659, another acyltransferase, PapA1, transfers one multiple methyl-branched (hydroxy) phthioceranoic acid to the 3'-position of SL659 to form SL1278, additional catalytic steps are acylation at the 6- and 6'-positions of SL1278 with two multiple methyl-branched (hydroxy) phthioceranoic acids, most likely through membrane-associated Chp1 to produce fully elaborated SL-1. These multiple methyl-branched (hydroxy) phthioceranoic acids are synthesized by polyketide synthase 2 (Pks2) using an activated fatty acid starter unit provided by fatty acyl AMP ligase FadD23 (FAAL23)
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physiological function
enzyme FadD23, together with Pks2, plays a central role in SL-1 synthesis. FAD23 belongs to a class of FadDs that comprises FAALs involved in the biosynthesis of toxic lipids in mycobacteria, as well as in the biosynthesis of lipopeptides of pharmaceutical importance in other microorganisms. It has been showsn that FAALs activate and transfer fatty acids onto related Pks proteins to further synthesize the diverse Mycobacterium tuberculosis lipids. FAALs use a carboxylate substrate and ATP to form acyl-AMP
physiological function
-
enzyme FadD23, together with Pks2, plays a central role in SL-1 synthesis. FAD23 belongs to a class of FadDs that comprises FAALs involved in the biosynthesis of toxic lipids in mycobacteria, as well as in the biosynthesis of lipopeptides of pharmaceutical importance in other microorganisms. It has been showsn that FAALs activate and transfer fatty acids onto related Pks proteins to further synthesize the diverse Mycobacterium tuberculosis lipids. FAALs use a carboxylate substrate and ATP to form acyl-AMP
-
physiological function
-
enzyme FadD23, together with Pks2, plays a central role in SL-1 synthesis. FAD23 belongs to a class of FadDs that comprises FAALs involved in the biosynthesis of toxic lipids in mycobacteria, as well as in the biosynthesis of lipopeptides of pharmaceutical importance in other microorganisms. It has been showsn that FAALs activate and transfer fatty acids onto related Pks proteins to further synthesize the diverse Mycobacterium tuberculosis lipids. FAALs use a carboxylate substrate and ATP to form acyl-AMP
-
additional information
FadDs adopt two main conformations: adenylation and thiolation forms. The C-terminal domains undergo a domain alternation of approximately 140° to complete the catalysis steps. The active site is located at the interface of the N- and C-terminal domains. Importance of the enzyme's C-terminal domain in the catalytic mechanism, substrate binding site structure, and dynamics of the catalytic cycle, overview
additional information
-
FadDs adopt two main conformations: adenylation and thiolation forms. The C-terminal domains undergo a domain alternation of approximately 140° to complete the catalysis steps. The active site is located at the interface of the N- and C-terminal domains. Importance of the enzyme's C-terminal domain in the catalytic mechanism, substrate binding site structure, and dynamics of the catalytic cycle, overview
-
additional information
-
FadDs adopt two main conformations: adenylation and thiolation forms. The C-terminal domains undergo a domain alternation of approximately 140° to complete the catalysis steps. The active site is located at the interface of the N- and C-terminal domains. Importance of the enzyme's C-terminal domain in the catalytic mechanism, substrate binding site structure, and dynamics of the catalytic cycle, overview
-
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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). FAA23_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
584
2
62841
Swiss-Prot
-
FAA23_MYCTO
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
584
2
62841
Swiss-Prot
-
FAA23_MYCBO
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
584
2
62841
Swiss-Prot
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
SDS-PAGE, gel filtration, and analytical ultracentrifugation
monomer
-
SDS-PAGE, gel filtration, and analytical ultracentrifugation
-
monomer
-
SDS-PAGE, gel filtration, and analytical ultracentrifugation
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme FadD23 bound to ATP and AMP-NPP. For holo-FadD23 crystals by mixing of 0.001 ml of 8 mg/ml protein FadD23, 2 mM ATP, and 2 mM MgCl2, with 0.001 ml of well solution containing 140 mM sodium citrate tribasic dihydrate, 60 mM magnesium chloride hexahydrate, 30 mM tris hydrochloride, pH 8.5, 14% w/v PEG 3350, and 9% w/v PEG 4000. For crystals of AMP-PNP-FadD23 complex 0.001 ml of protein solution is mixed with 70 mM Tris, pH 8.5, 140 mM sodium citrate tribasic dihydrate, 140 mM ammonium phosphate monobasic, 35% w/v (+/?)-2-methyl-2,4-pentanediol, and 14% w/v PEG 3350. The crystal of the FadD23 N-terminal domain suitable for diffraction experiments ar foemd by mixing of protein solution with 70 mM Bis-Tris pH 6.5, 60 mM sodium chloride, 20% w/v PEG 3350, and 6% w/v PEG 6000. X-ray diffraction structure determination and analysis at 2.25-2.68 A resolution. Apo-FadD23 only yield poor-quality crystals that do not produce usable diffraction data
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D446A
site-directed mutagenesis, no obvious protein expression
F192S
site-directed mutagenesis, no obvious protein expression
F265S
site-directed mutagenesis, no obvious protein expression
H221A
site-directed mutagenesis, the mutant shows 25% reduced activity compared to wild-type
M195S
site-directed mutagenesis, no obvious protein expression
S300A
site-directed mutagenesis, no obvious protein expression
F192S
-
site-directed mutagenesis, no obvious protein expression
-
F265S
-
site-directed mutagenesis, no obvious protein expression
-
H221A
-
site-directed mutagenesis, the mutant shows 25% reduced activity compared to wild-type
-
M195S
-
site-directed mutagenesis, no obvious protein expression
-
S300A
-
site-directed mutagenesis, no obvious protein expression
-
H221A
-
site-directed mutagenesis, the mutant shows 25% reduced activity compared to wild-type
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene fadD23, recombinant expression of wild-type and mutant enzymes in Mycobacterium smegmatis and in Escherichia coli. FadD23 directly captures palmitic acid from the Escherichia coli expression system
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Park, I.K.; Hsu, A.P.; Tettelin, H.; Shallom, S.J.; Drake, S.K.; Ding, L.; Wu, U.I.; Adamo, N.; Prevots, D.R.; Olivier, K.N.; Holland, S.M.; Sampaio, E.P.; Zelazny, A.M.
Clonal diversification and changes in lipid traits and colony morphology in Mycobacterium abscessus clinical isolates
J. Clin. Microbiol.
53
3438-3447
2015
Mycobacteroides abscessus
brenda
Lynett, J.; Stokes, R.W.
Selection of transposon mutants of Mycobacterium tuberculosis with increased macrophage infectivity identifies fadD23 to be involved in sulfolipid production and association with macrophages
Microbiology
153
3133-3140
2007
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Gokhale, R.; Saxena, P.; Chopra, T.; Mohanty, D.
Versatile polyketide enzymatic machinery for the biosynthesis of complex mycobacterial lipids
Nat. Prod. Rep.
24
267-277
2007
Mycobacterium tuberculosis
brenda
Yan, M.; Cao, L.; Zhao, L.; Zhou, W.; Liu, X.; Zhang, W.; Rao, Z.
The key roles of Mycobacterium tuberculosis FadD23C-terminal domain in catalytic mechanisms
Front. Microbiol.
14
1090534
2023
Mycobacterium tuberculosis (P9WQ47), Mycobacterium tuberculosis ATCC 25618 (P9WQ47), Mycobacterium tuberculosis H37Rv (P9WQ47)
brenda
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