Dipeptide: A dipeptide is a sometimes ambiguous designation of two classes of organic compounds: Its molecules contain either two amino acids joined by a single peptide bond or one amino acid with two peptide bonds.CarnosineProlidase deficiency: Prolidase deficiency (PD) is an autosomal recessive disease that is extremely uncommon and is associated with collagen metabolism and affects the connective tissues. This rare condition affects assorted systems because of an error on an enzyme, which is affiliated with the creation of collagen.NLRC3: NLRC3, short for NOD-like receptor family CARD domain containing 3, is an intracellular protein that plays a role in the immune system. It was previously known as nucleotide-binding oligomerization domain, leucine rich repeat and CARD domain containing 3 (NOD3) and CLR16.GlycylglycineDiketopiperazine: A diketopiperazine (DKP), also known as a dioxopiperazine or piperazinedione, is a class of organic molecules in which the two nitrogen atoms of a piperazine 6-membered ring are part of amide linkages. There are three regioisomers possible, differing in the locations of the two carbonyl groups around the ring.Electroneutral cation-Cl: In molecular biology, the electroneutral cation-Cl (electroneutral potassium-chloride cotransporter) family of proteins are a family of solute carrier proteins. This family includes the products of the Human genes: SLC12A1, SLC12A1, SLC12A2, SLC12A3, SLC12A4, SLC12A5, SLC12A6, SLC12A7, SLC12A8 and SLC12A9.RGD motifProteinogenic amino acid: Proteinogenic amino acids are amino acids that are precursors to proteins, and are incorporated into proteins cotranslationally — that is, during translation. There are 23 proteinogenic amino acids in prokaryotes (including N-Formylmethionine, mainly used to initiate protein synthesis and often removed afterward), but only 21 are encoded by the nuclear genes of eukaryotes.Glycine (plant): Glycine is a genus in the bean family Fabaceae. The best known species is the soybean (Glycine max).Protein primary structure: The primary structure of a peptide or protein is the linear sequence of its amino acid structural units, and partly comprises its overall biomolecular structure. By convention, the primary structure of a protein is reported starting from the amino-terminal (N) end to the carboxyl-terminal (C) end.Specificity constant: In the field of biochemistry, the specificity constant (also called kinetic efficiency or k_{cat}/K_{M}), is a measure of how efficiently an enzyme converts substrates into products. A comparison of specificity constants can also be used as a measure of the preference of an enzyme for different substrates (i.CefadroxilSEA Native Peptide LigationCefalexinColes PhillipsBurst kinetics: Burst kinetics is a form of enzyme kinetics that refers to an initial high velocity of enzymatic turnover when adding enzyme to substrate. This initial period of high velocity product formation is referred to as the "Burst Phase".Mediated transportCodinaeopsinImmunologic adjuvant: In immunology, an adjuvant is a component that potentiates the immune responses to an antigen and/or modulates it towards the desired immune responses. The word “adjuvant” comes from the Latin word adiuvare, meaning to help or aid.Ethyl groupUbenimexSharpless asymmetric dihydroxylation: Sharpless asymmetric dihydroxylation (also called the Sharpless bishydroxylation) is the chemical reaction of an alkene with osmium tetroxide in the presence of a chiral quinine ligand to form a vicinal diol.Alkaliphile: Alkaliphiles are a class of extremophilic microbes capable of survival in alkaline (pH roughly 8.5-11) environments, growing optimally around a pH of 10.Proline-Rich Coiled Coil 1: Proline Rich Coiled Coil-1 (PRCC1) is the commonly identified protein name of CAD38605. The PRCC1 gene is found on the long arm of Chromosome 5.Peptidoglycan binding domainDipeptidyl-peptidase IV family: In molecular biology, the dipeptidyl-peptidase IV family is a family of serine peptidases which belong to MEROPS peptidase family S9 (clan SC), subfamily S9B (dipeptidyl-peptidase IV). The protein fold of the peptidase domain for members of this family resembles that of serine carboxypeptidase D, the type example of clan SC.NACHT domain: NACHT is an acronym standing for NAIP (neuronal apoptosis inhibitor protein), C2TA (MHC class 2 transcription activator), HET-E (incompatibility locus protein from Podospora anserina) and TP1 (telomerase-associated protein). The NACHT domain is an evolutionarily conserved protein domain.Cord factor: Cord factor, or trehalose dimycolate, is a glycolipid molecule found in the cell wall of Mycobacterium tuberculosis and similar species. It is the primary lipid found on the exterior of M.JejunumList of strains of Escherichia coli: Escherichia coli is a well studied bacterium that was first identified by Theodor Escherich, after whom it was later named.Tripartite ATP-independent periplasmic transporter: Tripartite ATP-independent periplasmic transporters (TRAP transporters) are a large family of solute transporters found in bacteria and archaea, but not in eukaryotes, that appear to be specific for the uptake of organic acids. They are unique in that they utilize a substrate binding protein (SBP) in combination with a secondary transporter.Phenylalanine N-monooxygenase: Phenylalanine N-monooxygenase (, phenylalanine N-hydroxylase, CYP79A2) is an enzyme with system name L-phenylalanine,NADPH:oxygen oxidoreductase (N-hydroxylating). This enzyme catalyses the following chemical reactionIminoglycinuriaReaction coordinateLeucyl aminopeptidase: Leucyl aminopeptidases (, leucine aminopeptidase, LAPs, leucyl peptidase, peptidase S, cytosol aminopeptidase, cathepsin III, L-leucine aminopeptidase, leucinaminopeptidase, leucinamide aminopeptidase, FTBL proteins, proteinates FTBL, aminopeptidase II, aminopeptidase III, aminopeptidase I) are enzymes that preferentially catalyze the hydrolysis of leucine residues at the N-terminus of peptides and proteins. Other N-terminal residues can also be cleaved, however.