Information on EC 2.3.1.181 -

Information on EC 2.3.1.181 - lipoyl(octanoyl) transferase:

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EC NUMBER	COMMENTARY
2.3.1.181	-

RECOMMENDED NAME	GeneOntology No.
lipoyl(octanoyl) transferase	GO:0033819

REACTION	REACTION DIAGRAM	COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
an octanoyl-[acyl-carrier protein] + a protein = a protein N6-(octanoyl)lysine + an [acyl-carrier protein]		-	-	-	-
an octanoyl-[acyl-carrier protein] + a protein = a protein N6-(octanoyl)lysine + an [acyl-carrier protein]		enzyme functions as a cysteine/lysine dyad acyltransferase, where K142 and C176 are acid/base catalysts. Reaction proceeds via an internal thioester intermediate	Mycobacterium tuberculosis	Q10404	676872

REACTION TYPE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
Acyl group transfer	Escherichia coli	-	-	662098
Acyl group transfer	Bos taurus	O46419	-	688368

PATHWAY	KEGG Link	MetaCyc Link
lipoate biosynthesis and incorporation I	-	PWY0-501
lipoate biosynthesis and incorporation III (Bacillus)	-	PWY-6987

SYSTEMATIC NAME

IUBMB Comments

octanoyl-[acyl-carrier protein]:protein N-octanoyltransferase

This is the first committed step in the biosynthesis of lipoyl cofactor. Lipoylation is essential for the function of several key enzymes involved in oxidative metabolism, as it converts apoprotein into the biologically active holoprotein. Examples of such lipoylated proteins include pyruvate dehydrogenase (E2 domain), 2-oxoglutarate dehydrogenase (E2 domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein) [2,3]. Lipoyl-ACP can also act as a substrate [4] although octanoyl-ACP is likely to be the true substrate [6] . The other enzyme involved in the biosynthesis of lipoyl cofactor is EC 2.8.1.8, lipoyl synthase. An alternative lipoylation pathway involves EC 2.7.7.63, lipoate---protein ligase, which can lipoylate apoproteins using exogenous lipoic acid (or its analogues).

SYNONYMS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
bLT	Bos taurus	O46419	-	688368
LIP2	Arabidopsis thaliana	-	-	663062
LipB	Escherichia coli	-	-	661184, 662002, 662098, 663308, 712504
LipB	Neurospora crassa, Pisum sativum	-	-	662098
LipB	Mycobacterium tuberculosis	Q10404	-	676872
LipB	Plasmodium falciparum	-	-	706425
LipB octanoyltransferase	Escherichia coli	-	-	704311
LipM	Bacillus subtilis	-	-	711217
lipoate/octanoate transferase	Escherichia coli	-	-	662098
lipoyl (octanoyl)-acyl carrier protein:protein transferase	Escherichia coli	-	-	662002, 662098
lipoyl(octanoyl) transferase	Bos taurus	O46419	-	688368
lipoyl(octanoyl)-[acyl-carrier-protein]-protein N-lipoyltransferase	Escherichia coli	-	-	662098
lipoyl(octanoyl)transferase	Escherichia coli	-	-	662098, 663308
lipoyltransferase	Escherichia coli	-	-	662098
lipoyltransferase	Bos taurus	O46419	-	688368
octanoyl (lipoyl): N-octanoyl (lipoyl) transferase	Plasmodium falciparum	-	-	706425
octanoyl-[acyl carrier protein {ACP}]:protein N-octanoyltransferase	Escherichia coli	-	-	704311
octanoyl-[acyl carrier protein]-protein N-octanoyltransferase	Escherichia coli	-	-	662098
octanoyl-[acyl carrier protein]:protein N-octanoyltransferase	Escherichia coli	-	-	661184
octanoyltransferase LipM	Bacillus subtilis	-	-	711217

CAS REGISTRY NUMBER	COMMENTARY
392687-64-8	-

ORGANISM	COMMENTARY	LITERATURE	SEQUENCE CODE	SEQUENCE DB	SOURCE
Arabidopsis thaliana	Columbia ecotype	663062	-	-
Bacillus subtilis	-	711217	-	-
Bos taurus	-	688368	O46419	UniProt
Escherichia coli	-	661184, 661982, 662002, 662098, 663308, 712504	-	-
Escherichia coli	wild type and several LipB knockout strains	704311	-	-
Mycobacterium tuberculosis	enzyme is considerably upregulated in patients with multiple-drug-resistant Mycobacterium tuberculosis	676872	Q10404	Uniprot
Neurospora crassa	-	662098	-	-
Pisum sativum	-	662098	-	-
Plasmodium falciparum	-	706425	-	-

GENERAL INFORMATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
metabolism	Escherichia coli	-	The LipB octanoyltransferase catalyzes the first step of lipoic acid synthesis in Escherichia coli, transfer of the octanoyl moiety from octanoyl-acyl carrier protein to the lipoyl domains of the E2 subunits of the 2-oxoacid dehydrogenases of aerobic metabolism.	704311
metabolism	Plasmodium falciparum	-	The apicoplast-specific LipB is dispensable for parasite growth due to functional redundancy of the parasite�s lipoic acid/octanoic acid ligases/transferases.	706425
physiological function	Escherichia coli	-	LipB (EC 2.3.11.181) is responsible for octanoylation of the E2 components of 2-oxoacid dehydrogenases to provide the substrates of LipA (EC 2.7.7.63), an S-adenosyl-L-methionine radical enzyme that inserts two sulfur atoms into the octanoyl moiety to give the active lipoylated dehydrogenase complexes	712504

SUBSTRATE	PRODUCT	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY/ Substrate	LITERATURE/ Substrate	COMMENTARY/ Product	LITERATURE/ Product	Reversibility r=reversible ir=irreversible ?=not specified
lipoyl-[acyl-carrier protein] + apo-pyruvate dehydrogenase protein	?		Escherichia coli	-	-	662002	-	-	?
octanoyl-[acyl-carrier protein] + a protein	a protein N6-(octanoyl)lysine + an [acyl-carrier protein]		Bacillus subtilis	-	-	711217	-	-	?
octanoyl-[acyl-carrier protein] + a protein	a protein N6-(octanoyl)lysine + an [acyl-carrier protein]		Escherichia coli	-	LipB (EC 2.3.11.181) is responsible for octanoylation of the E2 components of 2-oxoacid dehydrogenases to provide the substrates of LipA (EC 2.7.7.63), an S-adenosyl-L-methionine radical enzyme that inserts two sulfur atoms into the octanoyl moiety to give the active lipoylated dehydrogenase complexes. LipB accumulates an octanoyl-enzyme intermediate with no sign of a lipoyl-enzyme intermediate, LipB (EC 2.3.11.181) is responsible for octanoylation of the E2 components of 2-oxoacid dehydrogenases to provide the substrates of LipA (EC 2.7.7.63), an S-adenosyl-L-methionine radical enzyme that inserts two sulfur atoms into the octanoyl moiety to give the active lipoylated dehydrogenase complexes. The binding sites for LipB reside both in the lipoyl domain and catalytic core sequences	712504	-	-	?
octanoyl-[acyl-carrier protein] + a protein	a protein N6-(octanoyl)lysine + an [acyl-carrier protein]		Bacillus subtilis	-	the transfer of the octanoyl group from octanoyl-ACP to Bacillus subtilis GcvH occurrs in a LipM-dependent manner. The LipM reaction proceeds through a thioester-linked acyl enzyme intermediate. The LipM active site nucleophile is identified as C150	711217	-	-	?
octanoyl-[acyl-carrier protein] + apo-E2 domain	apo E2-domain protein N6-(octanoyl)lysine + acyl-carrier protein		Escherichia coli	-	reaction proceeds through an acyl-enzyme intermediate	661184	-	-	?
octanoyl-[acyl-carrier protein] + apo-H protein	APO H-protein N6-(octanoyl)lysine + acyl-carrier protein		Escherichia coli	-	LipB reaction represents the first committed step in the biosynthesis of the lipoyl cofactor. apo-H protein is the lipoyl bearing subunit of the glycine cleavage system	663308	-	-	?
octanoyl-[acyl-carrier protein] + apo-H protein	apo-H protein N6-(octanoyl)lysine + acyl-carrier protein		Escherichia coli	-	apo-H protein is the lipoyl bearing subunit of the glycine cleavage system	663308	-	-	?
octanoyl-[acyl-carrier protein] + apo-pyruvate dehydogenase protein	apo-pyruvate dehydrogenase protein N6-(octanoyl)lysine + acyl-carrier protein		Escherichia coli	-	-	662002	-	-	?
octanoyl-[acyl-carrier protein] + protein	protein N6-(octanoyl)lysine + acyl-carrier protein		Escherichia coli	-	-	661184, 662098	-	-	?
octanoyl-[acyl-carrier protein] + protein	protein N6-(octanoyl)lysine + acyl-carrier protein		Neurospora crassa, Pisum sativum	-	-	662098	-	-	?
octanoyl-[acyl-carrier protein] + protein	protein N6-(octanoyl)lysine + acyl-carrier protein		Escherichia coli	-	first committed step in the biosynthesis of lipoyl cofactor. The lipoyl cofactor is essential for the function of glycine cleavage system (H protein)	661982	-	-	?
octanoyl-[acyl-carrier protein] + protein	protein N6-(octanoyl)lysine + acyl-carrier protein		Escherichia coli, Neurospora crassa, Pisum sativum	-	first committed step in the biosynthesis of lipoyl cofactor. The lipoyl cofactor is essential for the function of pyruvate dehydrogenase (E2 domain)	662098	-	-	?
octanoyl-[acyl-carrier protein] + protein	protein N6-(octanoyl)lysine + acyl-carrier protein		Arabidopsis thaliana	-	first committed step in the biosynthesis of lipoyl cofactor. The lipoyl cofactor is essential for the function of pyruvate dehydrogenase (E2 domain) and of the 2-oxoglutarate dehydrogenase complex	663062	-	-	?
octanoyl-[acyl-carrier protein] + protein	protein N6-(octanoyl)lysine + [acyl-carrier protein]		Bos taurus	O46419	-	688368	-	-	?

NATURAL SUBSTRATES	NATURAL PRODUCTS	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY SUBSTRATE	LITERATURE (Substrate)	COMMENTARY PRODUCT	LITERATURE (Product)
octanoyl-[acyl-carrier protein] + a protein	a protein N6-(octanoyl)lysine + an [acyl-carrier protein]		Bacillus subtilis	-	-	711217	-	-
octanoyl-[acyl-carrier protein] + a protein	a protein N6-(octanoyl)lysine + an [acyl-carrier protein]		Escherichia coli	-	LipB (EC 2.3.11.181) is responsible for octanoylation of the E2 components of 2-oxoacid dehydrogenases to provide the substrates of LipA (EC 2.7.7.63), an S-adenosyl-L-methionine radical enzyme that inserts two sulfur atoms into the octanoyl moiety to give the active lipoylated dehydrogenase complexes. LipB accumulates an octanoyl-enzyme intermediate with no sign of a lipoyl-enzyme intermediate	712504	-	-
octanoyl-[acyl-carrier protein] + apo-H protein	APO H-protein N6-(octanoyl)lysine + acyl-carrier protein		Escherichia coli	-	LipB reaction represents the first committed step in the biosynthesis of the lipoyl cofactor. apo-H protein is the lipoyl bearing subunit of the glycine cleavage system	663308	-	-
octanoyl-[acyl-carrier protein] + protein	protein N6-(octanoyl)lysine + acyl-carrier protein		Escherichia coli	-	-	661184	-	-
octanoyl-[acyl-carrier protein] + protein	protein N6-(octanoyl)lysine + acyl-carrier protein		Escherichia coli	-	first committed step in the biosynthesis of lipoyl cofactor. The lipoyl cofactor is essential for the function of glycine cleavage system (H protein)	661982	-	-
octanoyl-[acyl-carrier protein] + protein	protein N6-(octanoyl)lysine + acyl-carrier protein		Escherichia coli, Neurospora crassa, Pisum sativum	-	first committed step in the biosynthesis of lipoyl cofactor. The lipoyl cofactor is essential for the function of pyruvate dehydrogenase (E2 domain)	662098	-	-
octanoyl-[acyl-carrier protein] + protein	protein N6-(octanoyl)lysine + acyl-carrier protein		Arabidopsis thaliana	-	first committed step in the biosynthesis of lipoyl cofactor. The lipoyl cofactor is essential for the function of pyruvate dehydrogenase (E2 domain) and of the 2-oxoglutarate dehydrogenase complex	663062	-	-
octanoyl-[acyl-carrier protein] + protein	protein N6-(octanoyl)lysine + [acyl-carrier protein]		Bos taurus	O46419	-	688368	-	-

COFACTOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

METALS and IONS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

INHIBITORS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
Octanoyl-CoA	Escherichia coli	-	0.5 mM, 67% inhibition	663308	2D-image

ACTIVATING COMPOUND	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
KHCO3	Escherichia coli	-	100 mM, slight activation	663308	2D-image
NaOAc	Escherichia coli	-	100 mM, slight activation	663308	2D-image

KM VALUE [mM]	KM VALUE [mM] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.0132	-	apo-H protein	Escherichia coli	-	pH 7.2, 37�C	663308	-
0.001	-	lipoyl-[acyl-carrier protein]	Escherichia coli	-	-	662002	2D-image
0.0102	-	octanoyl-[acyl-carrier protein]	Escherichia coli	-	pH 7.2, 37�C	663308	2D-image

TURNOVER NUMBER [1/s]	TURNOVER NUMBER MAXIMUM[1/s]	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.2	-	apo-H protein	Escherichia coli	-	pH 7.2, 37�C	663308	-
0.2	-	octanoyl-[acyl-carrier protein]	Escherichia coli	-	pH 7.2, 37�C	663308	2D-image

kcat/KM VALUE [1/mMs^-1]	kcat/KM VALUE [1/mMs^-1] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

Ki VALUE [mM]	Ki VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

IC50 VALUE [mM]	IC50 VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg]	SPECIFIC ACTIVITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
0.54	-	Escherichia coli	-	-	663308

pH OPTIMUM	pH MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
7	-	Bacillus subtilis	-	assay at	711217
7.5	-	Escherichia coli	-	-	663308
7.8	-	Bos taurus	O46419	assay of lipoylation	688368

pH RANGE	pH RANGE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
6	9	Escherichia coli	-	pH 6.0: about 65% of maximal activity, pH 9.0: about 40% of maximal activity	663308

TEMPERATURE OPTIMUM	TEMPERATURE OPTIMUM MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
37	-	Bos taurus	O46419	assay of lipoylation	688368
37	-	Bacillus subtilis	-	assay at	711217

TEMPERATURE RANGE	TEMPERATURE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

pI VALUE	pI VALUE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

SOURCE TISSUE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	SOURCE
leaf	Arabidopsis thaliana	-	-	663062
liver	Bos taurus	O46419	-	688368

LOCALIZATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	GeneOntology No.	LITERATURE	SOURCE
mitochondrion	Neurospora crassa, Pisum sativum	-	-	5739	662098
mitochondrion	Arabidopsis thaliana	-	-	5739	663062
mitochondrion	Bos taurus	O46419	-	5739	688368

PDB	SCOP	CATH	ORGANISM
No entries in this field

MOLECULAR WEIGHT	MOLECULAR WEIGHT MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
10000	-	Escherichia coli	-	monomer, gel filtration	663308
14000	-	Bacillus subtilis	-	gel filtration	711217
26220	-	Escherichia coli	-	MALDI mass spectrometry	712504
29000	-	Escherichia coli	-	trimer, gel filtration	663308

SUBUNITS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
monomer	Bacillus subtilis	-	1 * 14000, SDS-PAGE	711217

POSTTRANSLATIONAL MODIFICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

Crystallization/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
the crystal structure of lipoyltransferase in complex with lipoyl-AMP is determined at a resolution of 2.1 A	Bos taurus	O46419	688368
enzyme shows thioether-linked active site complex with decanoic acid. Structural comparison with lipoate protein ligase A	Mycobacterium tuberculosis	Q10404	676872

pH STABILITY	pH STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

TEMPERATURE STABILITY	TEMPERATURE STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

GENERAL STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

ORGANIC SOLVENT	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

OXIDATION STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

STORAGE STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

Purification/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
-	Bacillus subtilis	-	711217
hydroxylapatite and DEAE-Sepharose columns are used for the purification of the recombinant protein and for the purification of lipoyltransferase from bovine liver mitochondria	Bos taurus	O46419	688368
-	Escherichia coli	-	662002
isolation and properties of a very stable complex between LipB and acyl cyrrier protein	Escherichia coli	-	712504
N-terminal hexahistidine-tagged apo-H protein	Escherichia coli	-	663308
wild-type and mutant His-tagged LipB proteins	Escherichia coli	-	661184

Cloned/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
-	Arabidopsis thaliana	-	663062
expression in Escherichia coli	Bacillus subtilis	-	711217
for expression in Escherichia coli BL21DE3 pLysS cells	Bos taurus	O46419	688368
-	Escherichia coli	-	712504
His-tagged LipB	Escherichia coli	-	662002
N-terminal hexahistidine-tagged apo-H protein	Escherichia coli	-	663308
wild-type and mutant His-tagged LipB proteins	Escherichia coli	-	661184

EXPRESSION	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

ENGINEERING	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
C150A	Bacillus subtilis	-	loss of the overall catalytic activity and an inability to form the acyl-enzyme intermediate	711217
C150S	Bacillus subtilis	-	loss of the overall catalytic activity and an inability to form the acyl-enzyme intermediate	711217
K165A	Bacillus subtilis	-	mutant has weakened catalytic ability	711217
K165R	Bacillus subtilis	-	mutant remains active	711217
C137A/C169A	Escherichia coli	-	mutant protein retains trace activity	661184
C169A	Escherichia coli	-	mutant enzyme retains trace activity, mutant enzyme forms an octanoyl-LpiB species that is not catalytically competent	661184
C169S	Escherichia coli	-	mutant enzyme has no activity, mutant enzyme forms an octanoyl-LpiB species that is not catalytically competent	661184
C169S	Escherichia coli	-	the hydrolyzed C169S mutant protein shows higher methyl octanoate levels than those of the wild type protein preparations	712504
additional information	Escherichia coli	-	Escherichia coli wild type strain and several spontaneous LipB knockout strains are used	704311

Renatured/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

APPLICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
medicine	Mycobacterium tuberculosis	Q10404	enzyme is considerably upregulated in patients with multiple-drug-resistant Mycobacterium tuberculosis	676872

REF.	AUTHORS	TITLE	JOURNAL	VOL.	PAGES	YEAR	ORGANISM	LINK TO PUBMED	SOURCE
661184	Zhao, X.; Miller, J.R.; Cronan, J.E.	The reaction of LipB, the octanoyl-[acyl carrier protein]:protein N-octanoyltransferase of lipoic acid synthesis, proceeds through an acyl-enzyme intermediate	Biochemistry	44	16737-16746	2005	Escherichia coli	PubMed
661982	vanden Boom, T.J.; Reed, K.E.; Cronan, J.E.	Lipoic acid metabolism in Escherichia coli: isolation of null mutants defective in lipoic acid biosynthesis, molecular cloning and characterization of the E. coli lip locus, and identification of the lipoylated protein of the glycine cleavage system	J. Bacteriol.	173	6411-6420	1991	Escherichia coli	PubMed
662002	Jordan, S.W.; Cronan, J.E., Jr.	The Escherichia coli lipB gene encodes lipoyl (octanoyl)-acyl carrier protein:protein transferase	J. Bacteriol.	185	1582-1589	2003	Escherichia coli	PubMed
662098	Jordan, S.W.; Cronan, J.E.	A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli	J. Biol. Chem.	272	17903-17906	1997	Escherichia coli, Neurospora crassa, Pisum sativum	PubMed
663062	Wada, M.; Yasuno, R.; Jordan, S.W.; Cronan, J.E., Jr.; Wada, H.	Lipoic acid metabolism in Arabidopsis thaliana: cloning and characterization of a cDNA encoding lipoyltransferase	Plant Cell Physiol.	42	650-656	2001	Arabidopsis thaliana	PubMed
663308	Nesbitt, N.M.; Baleanu-Gogonea, C.; Cicchillo, R.M.; Goodson, K.; Iwig, D.F.; Broadwater, J.A.; Haas, J.A.; Fox, B.G.; Booker, S.J.	Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase	Protein Expr. Purif.	39	269-282	2005	Escherichia coli	PubMed
676872	Ma, Q.; Zhao, X.; Nasser Eddine, A.; Geerlof, A.; Li, X.; Cronan, J.E.; Kaufmann, S.H.; Wilmanns, M.	The Mycobacterium tuberculosis LipB enzyme functions as a cysteine/lysine dyad acyltransferase	Proc. Natl. Acad. Sci. USA	103	8662-8667	2006	Mycobacterium tuberculosis	PubMed
688368	Fujiwara, K.; Hosaka, H.; Matsuda, M.; Okamura-Ikeda, K.; Motokawa, Y.; Suzuki, M.; Nakagawa, A.; Taniguchi, H.	Crystal structure of bovine lipoyltransferase in complex with lipoyl-AMP	J. Mol. Biol.	371	222-234	2007	Bos taurus	PubMed
704311	Hermes, F.A.; Cronan, J.E.	Scavenging of cytosolic octanoic acid by mutant LplA lipoate ligases allows growth of Escherichia coli strains lacking the LipB octanoyltransferase of lipoic acid synthesis	J. Bacteriol.	191	6796-6803	2009	Escherichia coli	PubMed
706425	Guenther, S.; Matuschewski, K.; Mueller, S.	Knockout studies reveal an important role of Plasmodium lipoic acid protein ligase A1 for asexual blood stage parasite survival	PLoS ONE	4	e5510	2009	Plasmodium falciparum	PubMed
711217	Christensen, Q.H.; Cronan, J.E.	Lipoic acid synthesis: a new family of octanoyltransferases generally annotated as lipoate protein ligases	Biochemistry	49	10024-10036	2010	Bacillus subtilis	PubMed
712504	Hassan, B.H.; Cronan, J.E.	Protein-protein interactions in assembly of lipoic acid on the 2-oxoacid dehydrogenases of aerobic metabolism	J. Biol. Chem.	286	8263-8276	2011	Escherichia coli	PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 2.3.1.181)

NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM

IUBMB Enzyme Nomenclature

PROSITE Database of protein families and domains

SYSTERS

Protein Mutant Database

InterPro (database of protein families, domains and functional sites)

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