Disease relevance of Glycyl-d-leucine

• Rates of absorption of leucine, glycylleucine, and glucose, and rates of hydrolysis of maltose were determined in the jejunum of a group of obese persons before and at intervals (between 2 and 20 montsh) after jejunoileal bypass for the treatment of obesity [1].
• Intestinal absorption of glycine 20 mmol/1, glycyl-glycine 10 mmol/1 plus L-leucine 10 mmol/1, and glycyl-L-leucine 10 mmol/1 has been studied by intestinal perfusion in 11 patients with tropical sprue and 10 control subjects [2].
• An in vivo effect of the metabolites L-alanine and glycyl-L-leucine on the properties of the lysyl-tRNA synthetase from Escherichia coli K-12. II. Kinetic evidence [3].

High impact information on Glycyl-d-leucine

• The substrate most discriminating for each enzyme is alpha-Glu-beta-naphthylamide for I (100% of the brush border activity for this substrate is due to enzyme I), glycylleucine for II (80%), leucyl-beta-naphthylamide for III (91%), and aspartyl-lysine in 5 mM Zn2+ for IV (63%) [4].
• The leucine absorption rate was significantly reduced after the bypass, but the absorption rates of glycylleucine and glucose as well as the hydrolysis rate of maltose were unchanged [1].
• Mechanisms of glycyl-L-leucine uptake by guinea-pig small intestine: relative importance of intact-peptide transport [5].
• 1. Characteristics of glycyl-L-leucine influx across the mucosal border of isolated guinea-pig ileum have been investigated [5].
• Overexpression of the yeaS gene encoding a protein belonging to the RhtB transporter family conferred upon cells resistance to glycyl-l-leucine, leucine analogues, several amino acids and their analogues. yeaS overexpression promoted leucine and, to a lesser extent, methionine and histidine accumulation by the respective producing strains [6].

Biological context of Glycyl-d-leucine

• The structure of the dipeptide binding protein in complex with Gly-Leu (glycyl-L-leucine) has been determined at 3.2 A resolution [7].
• 1. Rats were mated and at weekly intervals during pregnancy and lactation, and after weaning, the dipeptidase activity in the supernatant fraction from small intestinal mucosa extracts was determined for two dipeptides: glycyl-L-leucine dipeptidase (EC 3.4.3.2) AND L-alanyl-L-glutamic acid dipeptidase [8].
• The enhancing effect of Labrasol on cephalexin transport was similarly observed in in situ studies, and when 0.5% Labrasol was used in the presence of glycyl-L-leucine or L-alanyl-L-alanine, 60 or 46% enhancement of the active transport of cephalexin by Labrasol was obtained [9].

Anatomical context of Glycyl-d-leucine

• The influxes from the mucosal solution to the enterocytes were investigated for glycylglycine, glycyl-L-leucine, and their constituent amino acids in isolated intestinal segments from suckling (3 to 4 days), weanling (10 to 14 days), and adult guinea pigs [10].
• 4. There is no correlation between the effects of amino acids on glycyl-L-leucine uptake and hydrolysis of glycyl-L-leucine by either particulate or cytosol fraction [11].
• To define the interactions between the absorption of glycyl-L-sarcosine (Gly-Sar; .1 mM) and glycine, L-methionylglycine, glycyl-L-leucine, L-carnosine, or L-methionylglycyl-L-methionyl-L-methionine (each at 5 mM), ovine omasal epithelium was collected from eight wethers (average BW=69+/-8.2 kg) and mounted in parabiotic chambers [12].

Associations of Glycyl-d-leucine with other chemical compounds

• 1. In the vascularly perfused frog small intestine, the characteristics of the washout into the vascular bed of L-leucine and glycine have been investigated following loading either as free amino acids or as the dipeptide glycyl-L-leucine [13].
• 2) Both anserine and carnosine were partially hydrolyzed in vitro by the glycylleucine dipeptidase-containing fraction [14].
• The results conclusively demonstrated that both glycylleucine dipeptidase and proline dipeptidase are exclusively located in the cytosol of the enterocytes [15].
• Experiments on the coupling of glycyl-L-leucine and acetyl-L-leucine to these gels have shown a high pH-dependence of the bond formation between the support and the alpha-amino group (pH optimum 9.7); the coupling reaction between the epoxide group and the carboxyl group is practically pH-independent [16].

Gene context of Glycyl-d-leucine

• Glycyl-L-leucine (3 mM) usually enhanced lysyl-tRNA synthetase activity two- to threefold in wild-type cells but did not further stimulate the synthetase activity in metK mutants [17].
• Peptide-gap inhibitors: I. Competitive inhibition of aminopeptidase M by a hydrolytically resistant dipeptide analogue of glycylleucine [18].
• Alkaline phosphatase and glycyl-L-leucine dipeptidase were significantly depleted, whereas maltase activity was only marginally reduced, and leucine aminopeptidase activity was normal [19].
• An in vivo effect of the metabolites L-alanine and glycyl-L-leucine on the properties of lysyl-tRNA synthetase from Escherichia coli K-12. I. Influence on subunit composition and molecular weight distribution [20].
• Three kinds of boreal zone fish were investigated for gastrointestinal glycyl-L-leucine (GL) dipeptide cleaving activity as a function of feeding stage and seasonal changes [21].

Analytical, diagnostic and therapeutic context of Glycyl-d-leucine

• Cathepsin D and three dipeptidases versus leucyl-glycine, glycyl-L-leucine and glycyl-glycine) were assayed in serial, microtome prepared frozen sections (+/- 125 micrograms fresh weight) and related to histological composition (Nissl stain), dry weight, total protein, and DNA content [22].

References