H-Leu-D-Leu-OH
H-Leu-D-Leu-OH structure
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Common Name | H-Leu-D-Leu-OH | ||
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| CAS Number | 17665-02-0 | Molecular Weight | 244.33100 | |
| Density | 1.051g/cm3 | Boiling Point | 432.7ºC at 760 mmHg | |
| Molecular Formula | C12H24N2O3 | Melting Point | N/A | |
| MSDS | USA | Flash Point | 215.5ºC | |
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Transport and signaling via the amino acid binding site of the yeast Gap1 amino acid transceptor.
Nat. Chem. Biol. 5 , 45-52, (2009) Transporter-related nutrient sensors, called transceptors, mediate nutrient activation of signaling pathways through the plasma membrane. The mechanism of action of transporting and nontransporting transceptors is unknown. We have screened 319 amino acid anal... |
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Rapid analysis of peptides and amino acids by CE-ESI-MS using chemically modified fused-silica capillaries.
Electrophoresis 30 , 2273-2279, (2009) The objective of this study was to prepare a coated capillary to achieve rapid analysis of peptides and amino acids (AAs) by CE-ESI-MS. The coated capillary was prepared by chemical modification of the fused silica (FS) capillary with 2-acrylamido-2-methyl-1-... |
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The gamma/sigma1 and alpha/sigma2 hemicomplexes of clathrin adaptors AP-1 and AP-2 harbor the dileucine recognition site.
Mol. Biol. Cell 18 , 1887-1896, (2007) The clathrin adaptors AP-1 and AP-2 bind cargo proteins via two types of motifs: tyrosine-based Yxx phi and dileucine-based [DE]XXXL[LI]. Although it is well established that Yxx phi motifs bind to the mu subunits of AP-1 or AP-2, dileucine motifs have been r... |
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Two di-leucine-based motifs account for the different subcellular localizations of the human endothelin-converting enzyme (ECE-1) isoforms.
J. Cell Sci. 112 , 3115-3125, (1999) Endothelin-converting enzyme (ECE-1) is a type II integral membrane protein which plays a key role in the biosynthetic pathway of the vasoconstricting endothelins. Three ECE-1 isoforms, differing by their N-terminal cytoplasmic tails, are generated from a sin... |
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Dileucine motif is sufficient for internalization and synaptic vesicle targeting of vesicular acetylcholine transporter.
Traffic 8 , 512-522, (2007) Efficient cholinergic transmission requires accurate targeting of vesicular acetylcholine transporter (VAChT) to synaptic vesicles (SVs). However, the signals that regulate this vesicular targeting are not well characterized. Although previous studies suggest... |
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Effect of dipeptides on the growth of Oenococcus oeni in synthetic medium deprived of amino acids.
Curr. Microbiol. 49 , 361-365, (2004) Oenococcus oeni has numerous amino acid requirements for growth and dipeptides could be important for its nutrition. In this paper the individual or combined effect of dipeptides on growth of O. oeni X2L in synthetic media deficient in one or more amino acids... |
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Enantioselective molecular recognition between beta-sheets.
J. Am. Chem. Soc. 126(10) , 3062-3, (2004) This communication asks whether homochiral or heterochiral interaction is preferred between enantiomeric beta-sheets and finds that homochiral pairing is strongly preferred. Interactions between beta-sheets occur widely among proteins through pairing of the h... |
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Sorting of mannose 6-phosphate receptors mediated by the GGAs.
Science 292(5522) , 1712-6, (2001) The delivery of soluble hydrolases to lysosomes is mediated by the cation-independent and cation-dependent mannose 6-phosphate receptors. The cytosolic tails of both receptors contain acidic-cluster-dileucine signals that direct sorting from the trans-Golgi n... |
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Differential recognition of a dileucine-based sorting signal by AP-1 and AP-3 reveals a requirement for both BLOC-1 and AP-3 in delivery of OCA2 to melanosomes.
Mol. Biol. Cell 23(16) , 3178-92, (2012) Cell types that generate unique lysosome-related organelles (LROs), such as melanosomes in melanocytes, populate nascent LROs with cargoes that are diverted from endosomes. Cargo sorting toward melanosomes correlates with binding via cytoplasmically exposed s... |
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Cleavage of L-leucine-containing dipeptides by Clostridium butyricum.
Bioorg. Med. Chem. Lett. 9 , 109-112, (1999) The ability of Clostridium butyricum cultures to hydrolyze three L-leucine-containing dipeptides (Leu-Leu, Leu-Gly and Gly-Leu) in a synthetic minimal medium is demonstrated by using gas chromatography coupled with mass spectrometry. The 13C nuclear magnetic ... |