Protein Family Models

This entry represents the catalytic domain of a group of lipoyl ligases/lipoyltransferases, such as Lipoate-protein ligase A/B (LipA/B) from E.coli and mammalian lipoyltransferases [1-5]. These proteins catalyse the transfer of the lipoyl group from lipoyl-AMP to the specific lysine residue of lipoyl domains of lipoate-dependent enzymes. Lipoic acid is an essential cofactor of the alpha-ketoacid dehydrogenase complexes and the glycine cleavage system. Paper describing PDB structure 1w66. [1]. 16735476. The Mycobacterium tuberculosis LipB enzyme functions as a cysteine/lysine dyad acyltransferase. Ma Q, Zhao X, Nasser Eddine A, Geerlof A, Li X, Cronan JE, Kaufmann SH, Wilmanns M;. Proc Natl Acad Sci U S A. 2006;103:8662-8667. Paper describing PDB structure 1x2g. [2]. 16043486. Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site. Fujiwara K, Toma S, Okamura-Ikeda K, Motokawa Y, Nakagawa A, Taniguchi H;. J Biol Chem. 2005;280:33645-33651. Paper describing PDB structure 2ars. [3]. 16141198. Crystal structure of lipoate-protein ligase A bound with the activated intermediate: insights into interaction with lipoyl domains. Kim DJ, Kim KH, Lee HH, Lee SJ, Ha JY, Yoon HJ, Suh SW;. J Biol Chem. 2005;280:38081-38089. Paper describing PDB structure 2c7i. [4]. 16384580. Structure of a putative lipoate protein ligase from Thermoplasma acidophilum and the mechanism of target selection for post-translational modification. McManus E, Luisi BF, Perham RN;. J Mol Biol. 2006;356:625-637. Paper describing PDB structure 2e5a. [5]. 17570395. Crystal structure of bovine lipoyltransfer. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-21

This family includes biotin protein ligase, lipoate-protein ligase A and B. Biotin is covalently attached at the active site of certain enzymes that transfer carbon dioxide from bicarbonate to organic acids to form cellular metabolites. Biotin protein ligase (BPL) is the enzyme responsible for attaching biotin to a specific lysine at the active site of biotin enzymes. Each organism probably has only one BPL. Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon-amino group of the modified lysine [2]. Lipoate-protein ligase A (LPLA) catalyses the formation of an amide linkage between lipoic acid and a specific lysine residue in lipoate dependent enzymes [3]. The unusual biosynthesis pathway of lipoic acid is mechanistically intertwined with attachment of the cofactor [5]. [1]. 1409631. Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. Wilson KP, Shewchuk LM, Brennan RG, Otsuka AJ, Matthews BW;. Proc Natl Acad Sci USA 1992;89:9257-9261. A comprehensive review of biotinylation. [2]. 10470036. The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity. Chapman-Smith A, Cronan JE Jr;. Trends Biochem Sci 1999;24:359-363. [3]. 8206909. Identification of the gene encoding lipoate-protein ligase A of Escherichia coli. Molecular cloning and characterization of the lplA gene and gene product. Morris TW, Reed KE, Cronan JE Jr;. J Biol Chem 1994;269:16091-16100. [4]. 11106165. Lipoylating and biotinylating enzymes contain a homo. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

Catalyzes the transfer of the lipoyl/octanoyl moiety of lipoyl/octanoyl-ACP onto lipoate-dependent enzymes like pyruvate dehydrogenase and the glycine cleavage system H protein

Gene:

lipB

Date:

2021-08-12

lipoyl(octanoyl) transferase LipB catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes

Date:

2023-03-24

Catalyzes the transfer of the lipoyl/octanoyl moiety of lipoyl/octanoyl-ACP onto lipoate-dependent enzymes like pyruvate dehydrogenase and the glycine cleavage system H protein.

Gene:

lipB

Date:

2024-06-10