Reaction Process: Plant Reactome:R-OSA-1119436
Peptidoglycan biosynthesis I related metabolites
find 20 related metabolites which is associated with chemical reaction(pathway) Peptidoglycan biosynthesis I
ATP + L-Ala + UDP-N-acetylmuramate ⟶ ADP + Pi + UDP-N-acetylmuramoyl-L-alanine
D-Alanyl-D-alanine
The ATP-dependent carboxylate-amine/thiol ligase superfamily is known to contain enzymes catalyzing the formation of various types of peptide, one of which is d-alanyl-d-alanine.(PMID: 16030213). The glycopeptide antibiotic vancomycin acts by binding to the D-alanyl-D-alanine terminus of the cell wall precursor lipid II in the cytoplasmic membrane.(PMID: 17418637). D-alanine-D-alanine ligase from Thermotoga maritima ATCC 43589 (TmDdl) was a useful biocatalyst for synthesizing D-amino acid dipeptides.D-Alanine-D-alanine ligase (Ddl) catalyzes the biosynthesis of an essential bacterial peptidoglycan precursor D-alanyl-D-alanine and it represents an important target for development of new antibacterial drugs. (PMID: 17267218). D-Alanyl-D-alanine is a microbial metabolite. Alanyl-alanine, also known as ala-ala or A-a dipeptide, is a member of the class of compounds known as dipeptides. Dipeptides are organic compounds containing a sequence of exactly two alpha-amino acids joined by a peptide bond. Alanyl-alanine is soluble (in water) and a weakly acidic compound (based on its pKa). Alanyl-alanine can be found in chives, which makes alanyl-alanine a potential biomarker for the consumption of this food product. Alanyl-alanine can be found primarily in feces. Alanyl-alanine exists in all living organisms, ranging from bacteria to humans. Acquisition and generation of the data is financially supported in part by CREST/JST. D-Ala-D-Ala constitutes the terminus of the peptide part of the peptidoglycan monomer unit and is involved in the transpeptidation reaction as the substrate. D-Ala-D-Ala is catalyzed by D-Alanine-D-Alanine ligase. D-Ala-D-Ala is a bacterial endogenous metabolite[1][2].
Undecaprenyl phosphate
D-Alanine
Alanine is a nonessential amino acid made in the body from the conversion of the carbohydrate pyruvate or the breakdown of DNA and the dipeptides carnosine and anserine. It is highly concentrated in muscle and is one of the most important amino acids released by muscle, functioning as a major energy source. Plasma alanine is often decreased when the BCAA (Branched Chain Amino Acids) are deficient. This finding may relate to muscle metabolism. Alanine is highly concentrated in meat products and other high-protein foods like wheat germ and cottage cheese. Alanine is an important participant as well as regulator in glucose metabolism. Alanine levels parallel blood sugar levels in both diabetes and hypoglycemia, and alanine reduces both severe hypoglycemia and the ketosis of diabetes. It is an important amino acid for lymphocyte reproduction and immunity. Alanine therapy has helped dissolve kidney stones in experimental animals. Normal alanine metabolism, like that of other amino acids, is highly dependent upon enzymes that contain vitamin B6. Alanine, like GABA, taurine and glycine, is an inhibitory neurotransmitter in the brain. Alanine can be found in some Gram-positive bacteria (PMID:24752840). Amino acids are one of the most important molecules in living organisms, and most of them have a chiral carbon at a -position. In the higher animals, a large part of the naturally occurring amino acids is the L-form, and the stereoisomers (D-amino acids) had been believed to be rare. However, several D-amino acids have been found in mammals including humans, and their distributions, functions and origins have gradually been clarified. The D-alanine (D-Ala) amounts have also been reported to change in the case of diseases. Proteins of the frontal lobe white and gray matter of human brains, both normal and Alzheimer subjects, contain D-alanine at concentrations between 0.50 and 1.28 mumol/g of wet tissue, 50-70-times lower than the concentration of L-alanine. D-Alanine have been detected in the sera of both normal subjects and patients with renal dysfunction, and their concentrations were higher in the patients than in the normal subjects. (PMID: 16141519, 1450921, 8535409, 1426150, 1933416) [HMDB] KEIO_ID A011 D-Alanine is a weak GlyR (inhibitory glycine receptor) and PMBA agonist, with an EC50 of 9 mM for GlyR. D-Alanine is a weak GlyR (inhibitory glycine receptor) and PMBA agonist, with an EC50 of 9 mM for GlyR.
D-Glutamic acid
There are two forms of glutamic acid found in nature: L-glutamic acid and D-glutamic acid. D-glutamic acid, is not endogenously produced in higher mammals. It is found naturally primarily in the cell walls of certain bacteria. D-glutamate is also present in certain foods e.g., soybeans and also arises from the turnover of the intestinal tract microflora, whose cell walls contain significant D-glutamate. Unlike other D-amino acids, D-glutamate is not oxidized by the D-amino acid oxidases, and therefore this detoxification pathway is not available for handling D-glutamate. Likewise, D-glutamic acid, when ingested, largely escapes most deamination reactions (unlike the L-counterpart). Free D-glutamate is found in mammalian tissue at surprisingly high levels, with D-glutamate accounting for 9\\% of the total glutamate present in liver. D-glutamate is the most potent natural inhibitor of glutathione synthesis identified to date and this may account for its localization to the liver, since circulating D-glutamate may alter redox stabiity (PMID 11158923). Certain eels are known to use D-glutamic acid as a phermone for chemical communication. D-Glutamic acid has been found to be a metabolite of Lactobacillus (PMID: 22754309). There are two forms of glutamic acid found in nature: L-glutamic acid and D-glutamic acid. D-glutamic acid, is not endogenously produced in higher mammals. It is found naturally primarily in the cell walls of certain bacteria. D-glutamate is also present in certain foods e.g., soybeans and also arises from the turnover of the intestinal tract microflora, whose cell walls contain significant D-glutamate. Unlike other D-amino acids, D-glutamate is not oxidized by the D-amino acid oxidases, and therefore this detoxification pathway is not available for handling D-glutamate. Likewise, D-glutamic acid, when ingested, largely escapes most deamination reactions (unlike the L-counterpart). Free D-glutamate is found in mammalian tissue at surprisingly high levels, with D-glutamate accounting for 9\\% of the total glutamate present in liver. D-glutamate is the most potent natural inhibitor of glutathione synthesis identified to date and this may account for its localization to the liver, since circulating D-glutamate may alter redox stabiity (PMID 11158923). Certain eels are known to use D-glutamic acid as a phermone for chemical communication. [HMDB] D018377 - Neurotransmitter Agents > D018846 - Excitatory Amino Acids KEIO_ID G005
Coenzyme II
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UMP dianion
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Phosphonatoenolpyruvate
C3H2O6P-3 (164.95890219999998)
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[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-oxidophosphoryl]oxy-oxidophosphoryl] phosphate
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Adenosine-diphosphate
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UDP-N-acetyl-alpha-D-glucosamine
C17H25N3O17P2-2 (605.0659180000001)
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L-glutamate(1-)
An alpha-amino-acid anion that is the conjugate base of L-glutamic acid, having anionic carboxy groups and a cationic amino group
UDP-N-Acetylmuramoyl-L-alanyl-D-glutamic acid
C28H43N5O23P2 (879.1823988000001)
uridine 5-(3-{2-acetylamino-3-O-[(R)-1-carboxyethyl]-2-deoxy-D-glucopyranosyl} dihydrogen diphosphate)
C20H31N3O19P2 (679.1026956000001)
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine
C20H29N3O19P2 (677.0870464000001)