Disease relevance of Lanthionine L-

• Nisin is a small cationic lanthionine antibiotic produced by Lactococcus lactis [1].
• They are characterized by the unique amino acids lanthionine and methyllanthionine, introduced by means of dehydration of Ser/Thr residues followed by reaction of the resulting dehydro amino acids with cysteines to form thioether linkages [2].
• The lantibiotics are a rapidly expanding group of biologically active peptides produced by a variety of Gram-positive bacteria, and are so-called because of their content of the thioether amino acids lanthionine and beta-methyllanthionine [3].
• In another mutagenesis study a double mutation was introduced in the nisZ gene by replacing the codons for Met-17 and Gly-18 by codons for Gln and Thr, respectively, as in the third lanthionine ring of the related antimicrobial peptide subtilin from Bacillus subtilis [4].
• Demonstration of lanthionine as a natural constituent of the peptidoglycan of Fusobacterium nucleatum [5].

High impact information on Lanthionine L-

• Lantibiotics are ribosomally synthesized oligopeptide antibiotics that contain lanthionine bridges derived by the posttranslational modification of amino acid residues [6].
• Our results suggest that lantibiotic maturation and secretion occur at a membrane-associated multimeric lanthionine synthetase complex consisting of proteins NisB, NisC, and the ABC transporter molecules NisT [7].
• Comparison of gene sequence homologies between nisin and the other lanthionine antibiotics, subtilin and epidermin, indicated that they all evolved from a common ancestor [8].
• In this issue of Molecular Microbiology, Wiedemann and coworkers have made a big step towards understanding the mechanism of action of the two-component lanthionine-containing antibiotic lacticin 3147 [9].
• Lan-7 is a novel, chemically stable peptide structurally related to somatostatin that contains a lanthionine bridge between the two cysteines in the peptide; TT-232 is a less stable analogue containing a disulfide bridge [10].

Chemical compound and disease context of Lanthionine L-

• Mersacidin is a lanthionine-containing peptide antibiotic that shows a good in vivo efficiency against methicillin-resistant Staphylococcus aureus [11].

Biological context of Lanthionine L-

• A direct synthesis of the thioether bridged analog (1) of sandostatin (SMS 201,995) and several lanthionine hexa-, hepta-, and octapeptides was carried out by using the method of cyclization on an oxime resin (PCOR) followed by condensation reactions in solution [12].
• A series of cyclic somatostatin analogs containing a lanthionine bridge have been subjected to studies of structure-activity relationships [12].
• The biosynthetic gene cluster (12.3 kb) of mersacidin, a lanthionine-containing antimicrobial peptide, is located on the chromosome of the producer, Bacillus sp. strain HIL Y-85,54728 in a region that corresponds to 348 degrees on the chromosome of Bacillus subtilis 168 [13].
• Immediately downstream of bvi79A was a second, partial open reading frame encoding a peptide with significant homology to proteins which are believed to be involved in the synthesis of lanthionine residues [14].
• The N-terminal amino acid sequences of all three peptides were obtained and staphylococcins C55alpha and C55beta were shown to be lanthionine-containing (lantibiotic) molecules with molecular weights of 3,339 and 2,993, respectively [15].

Anatomical context of Lanthionine L-

• Characterization of rat LANCL1, a novel member of the lanthionine synthetase C-like protein family, highly expressed in testis and brain [16].
• Quantitation of cystathionine ketimine and lanthionine ketimine indicates a mean concentration (mean +/- SD, n = 4) of 2.3 +/- 0.8 nmol/g for CK and of 1.1 +/- 0.3 nmol/g for LK in four human cerebral cortex samples of neurosurgical source [17].
• Human peripheral blood polymorphonuclear leukocytes were preincubated with lanthionine, S-(2-aminoethyl)-L-cysteine, and some of their derivatives found in normal human urine and bovine brain [18].

Associations of Lanthionine L- with other chemical compounds

• [structure: see text] Lanthionine, a thioether analogue of cystine, is a key component of the lantibiotics, a family of modified peptides bearing multiple thioether bridges resulting from posttranslational modifications between side chains [19].
• As previously described, ketimines arise from the deamination of a number of sulfur-containing amino acids, i.e. L-cystathionine, L-lanthionine and S-aminoethyl-L-cysteine, catalyzed by a widespread mammalian transaminase [20].
• The NMR data were additionally confirmed by mass spectrometry and Edman degradation after chemical modification, which allowed sequencing of lanthionine and beta-methyllanthionine residues [21].
• The SH groups could be completely alkylated at pH 7.6 in aqueous propanol, as shown by nearly quantitative recovery of lanthionine [22].

Gene context of Lanthionine L-

• Therefore, lanthionine-based lipopeptide amides were synthesized and probed for activity as potential TLR2 agonists or antagonists [23].
• LANCL1 (LanC-like protein 1) is related to the bacterial LanC (lanthionine synthetase C) family, which is involved in the biosynthesis of antimicrobial peptides [24].
• Synthesis and biological activities of cyclic lanthionine enkephalin analogues: delta-opioid receptor selective ligands [25].
• Electron capture induced dissociation (ECD) and collisionally activated dissociation (CAD) experiments were performed on four lanthionine bridge-containing antibiotics [26].
• It was shown to be a 2,675-Da bacteriocin harboring a lanthionine structure [27].

Analytical, diagnostic and therapeutic context of Lanthionine L-

• A new sulfur imino acid, 2H-1,4-thiazine-5,6-dihydro-3,5-dicarboxylic acid (lanthionine ketimine), has been detected in the bovine brain by means of fluorometric and HPLC procedures [28].

References