6.3.1.20: lipoate-protein ligase

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For detailed information about lipoate-protein ligase, go to the full flat file.

Reaction

Synonyms

CTD, EC 2.7.7.63, LIP3, LipB, LipL1, lipoate ligase, lipoate ligase like protein, lipoate protein ligase, lipoate protein ligase B, lipoate-bound lipoate ligase 1, lipoate-protein ligase, lipoate-protein ligase A, lipoic acid ligase, lipoic acid ligase A, lipoic acid protein ligase, lipoic acid protein ligase A1, lipoyl ligase, lipoyl-protein ligase A, LPLA, LplA-LplB complex, LplA1, LplA1Ct, Lpla2, LplB, Oryza s. lipoate-protein ligase A, OsLPLA, PfLipL1

ECTree

     6 Ligases

         6.3 Forming carbon-nitrogen bonds

             6.3.1 Acid—ammonia (or amine) ligases (amide synthases)

                6.3.1.20 lipoate-protein ligase

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Results	in table
1	Activating Compound
10845	AA Sequence
5	Application
1	CAS Registry Number
14	Cloned(Commentary)
8	Cofactor
5	Crystallization (Commentary)
15	Disease/ Diagnostics
2	Expression
16	General Information
15	Inhibitors
4	kcat/KM [mM/s]
19	KM Value [mM]
10	Localization
18	Metals/Ions
13	Molecular Weight [Da]
18	Natural Substrates/ Products (Substrates)
43	Organism
1	Oxidation Stability
5	Pathway
2	PDB ID
4	pH Optimum
1	pH Range
2	pI Value
29	Protein Variants
11	Purification (Commentary)
4	Reaction
1	Reaction Type
35	Reference
1	Renatured (Commentary)
8	Source Tissue
5	Specific Activity [micromol/min/mg]
2	Storage Stability
71	Substrates and Products (Substrate)
8	Subunits
63	Synonyms
1	Systematic Name
5	Temperature Optimum [°C]
13	Turnover Number [1/s]

Crystallization

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Crystallization on EC 6.3.1.20 - lipoate-protein ligase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

alone and in complex with lipoic acid

Escherichia coli

-

665657

structural models of LplA1 and LplA2 based on Escherichia coli (PDB: 1X2H) and Streptococcus pneumoniae (PDB: 1VQZ) LplA proteins, conserved lipoyl-AMP binding pocket, LplA1: regions of clustered negatively charged residues, overall electrostatic potential of -13, LplA2: overall electrostatic potential of -5

Listeria monocytogenes

-

694219

structural comparison of lipoate-protein ligase with cysteine/lysine dyad acyltransferase LipB shows conserved structural and sequence active-site features, but 4’-phosphopantheine-bound octanoic acid recognition is a specific property of cysteine/lysine dyad acyltransferase

Mycobacterium tuberculosis

-

676872

purified recombinant lipoyl-PfLipL1D243-279 complex, mixing of 0.001 ml of 5 mg/ml protein, 1.2 mol equiv of lipoate, and excess ATP with 0.001 ml of reservoir solution containing 100 mM HEPES, pH 7.0, 1.5 M (NH4)2SO4, and 20% ethylene glycol, 20°C, method optimization, X-ray diffraction structure determination and analysis at 2.32 A resolution

Plasmodium falciparum

Q8IEG9

746406

as apo form, in complex with ATP, and as lipoyl-AMP-complex. Lipoyl-AMP is bound deeply in the bifurcated pocket and adopts a U-shaped conformation

Thermoplasma acidophilum

Q9HKT1

665675