â€œdl-Alanineâ€ Organic Syntheses, Collected Volume 1, p.21 (1941).
Alanine is found in a wide variety of foods, but is particularly concentrated in meats.
Alanine--glyoxylate aminotransferase 2, mitochondrial
In addition to the six known routes, other biochemically plausible routes to β-alanine were also examined. These include the reaction of acrylate and ammonia and the elimination of fumarate from N-(2-carboxyethyl)--aspartate. The acrylate and ammonia reaction produced no increase in the amount of β-alanine. Although a large increase in the amount of β-alanine in cell extracts was observed from incubating the cells with N-(2-carboxyethyl)--aspartate, this was likely catalyzed by adenylosuccinate lyase (MJ0929) present in the extracts. We have demonstrated that this enzyme catalyzes this reaction (data not shown). The origin of N-(2-carboxyethyl)--aspartate from a reaction of malonate semialdehyde with aspartate, followed by a reduction; from the reaction of acetyl-CoA, formaldehyde, and aspartate; from the reaction between acryloyl-CoA and aspartate; or from the reaction of acryloyl and aspartate could not be demonstrated (data not shown).
When normal alanine is irradiated, the radiation causes certain alanine molecules to become free radicals, and, as these radicals are stable, the free radical content can later be measured in order to find out how much radiation the alanine was exposed to.
Involved in the biosynthesis of alanine
Although the E. coli ΔpanD strain does not express T7 RNA polymerase, it has been observed that the protein encoded by the gene on the T7 promoter vector was expressed at a low but functional significant level in the absence of T7 RNA polymerase (). Therefore, the cells without addition of β-alanine were grown for 24 to 48 h due to the low protein expression level; the cells supplemented by β-alanine were grown for 12 to 18 h with constant agitation (250 rpm) at 37°C.
No increase in the amount of the 10 μM background level of β-alanine was observed when cell extracts were incubated with dihydrouracil, spermine, or α-alanine to test for reactions 3, 4, and 5, respectively, in . Similarly, no change in β-alanine concentration was observed when cell extracts were incubated with malonate semialdehyde, NADH, and NADPH to test for reaction 2 in .
L-alanine biosynthesis I, L-alanine degradation I: BR162 : R00401 : …
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Nonalcoholic fatty liver disease is suspected on the basis of various clinical aspects (an elevated alanine aminotransferase concentration, presence of obesity and diabetes) that alone are not sufficient to establish diagnosis or prognosis.
Showing metabocard for L-Alanine (HMDB0000161)
Amino acids biosynthesis and nitrogen assimilation pathways: ..
Alanine - Wikipedia
isoleucine and leucine biosynthesis and (B) a group of alanine …
The amino acid metabolism page details the synthesis and breakdown of essential and non-essential amino acids.
Alanine, aspartate and glutamate metabolism
Figure 2 shows the six known routes or pathways for the biosynthesis of β-alanine and ..
biosynthesis of more-complex molecules
This glucose is then taken up by resting muscles, red blood cells, and other tissues.
AST (Aspartate aminotransferase) U/L (5 to 45)
(Alanine aminotransferase) U/L (5 to 45)
Albumin g/L (38-55)
Clotting Studies (Prothrombin Time) Seconds (11 to 13.5)
Total Bilirubin - Normal range is 3 - 18 umol/L (0.17 - 1 mg/dL).
and is used today for making L-alanine.
Coenzyme A (CoA) is an important coenzyme in all known living organisms where it functions as an acyl carrier for amide-, ester-, and thioester-forming reactions as well as activating carbonyl groups for Claisen condensation reactions. Its biosynthetic pathway from the primary metabolites -aspartate, α-ketoisovalerate, the methylene group of 5,10-methylene-tetrahydrofolate, cysteine, and ATP has now been completely defined in bacteria and is known to require nine enzymes () (). Recently, an alternate pathway for the biosynthesis of -4′-phosphopantothenate was identified in Thermococcus kodakaraensis (). Here pantoic acid is first phosphorylated to form 4-phosphopantoic acid that in turn is coupled with β-alanine to form -4′-phosphopantothenate (, most archaea). In most archaea, the order of condensation of the β-alanine and phosphorylation reactions have been found to be reversed compared to the classical pathways in bacteria (). This discovery led to the identification of the pantoate kinase (MJ0969) and the phosphopantothenate synthetase (MJ0209) as the genes encoding these enzymes in Methanocaldococcus jannaschii. At present, the activities of the bifunctional phosphopantothenoylcysteine synthase encoded by MJ0913 (), the phosphopantotheine adenylyltransferase (MJ1030) from Pyrococcus abyssi (), the pantoate kinase (MJ0969) from Thermococcus kodakaraensis (, ), the phosphopantothenate synthetase (MJ0209) from both Thermococcus kodakaraensis () and Methanospirillum hungatei () have been confirmed experimentally.
predominant one when pyruvate or alanine is …
As a result, alanine aminotransferase (ALT or SGPT), aspartate aminotransferase (AST or SGOT), gamma-glutamyltransferase (GGT), alkaline phosphatase (ALP) and bilirubin have proven problematic for clinicians.
12.01.2013 · L -Alanine is second only ..
With this inventory of genes we are left with at least three genes/enzymes for CoA biosynthesis that needed to be identified in the methanogens. These include the enzymes for β-alanine and pantoic acid production. PanD, a pyruvoyl-containing enzyme, is responsible for catalyzing the decarboxylation of aspartate to β-alanine in bacteria (). Although pyruvoyl-containing enzymes are known in the methanogens (, ), no PanD homologs are present in methanogenic genomes. The canonical enzymes for pantoic acid biosynthesis require 5,10-methylene-tetrahydrofolate, which is absent in most archaeal methanogens (,). A likely alternate substrate for pantoic acid biosynthesis in the methanogens would be 5,10-methylene-tetrahydromethanopterin, since this cofactor can function in an analogous manner as 5,10-methylene-tetrahydrofolate as demonstrated by its involvement in serine metabolism using the archaeal version of serine hydroxymethyltransferase ().
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