| InChI=1S/C6H13NO2/c1-3-4(2)5(7)6(8)9/h4-5H,3,7H2,1-2H3,(H,8,9)/t4-,5-/m1/s1 |
| AGPKZVBTJJNPAG-RFZPGFLSSA-N |
| CC[C@@H](C)[C@@H](N)C(O)=O |
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Saccharomyces cerevisiae
(NCBI:txid4932)
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See:
PubMed
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Bronsted base
A molecular entity capable of accepting a hydron from a donor (Bronsted acid).
(via organic amino compound )
Bronsted acid
A molecular entity capable of donating a hydron to an acceptor (Bronsted base).
(via oxoacid )
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bacterial metabolite
Any prokaryotic metabolite produced during a metabolic reaction in bacteria.
Saccharomyces cerevisiae metabolite
Any fungal metabolite produced during a metabolic reaction in Baker's yeast (Saccharomyces cerevisiae ).
Daphnia magna metabolite
A Daphnia metabolite produced by the species Daphnia magna.
(via isoleucine )
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View more via ChEBI Ontology
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(2R,3R)-2-amino-3-methylpentanoic acid
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IUPAC
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(2R,3R)-2-Amino-3-methylvaleric acid
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KEGG COMPOUND
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(R)-2-Amino-(S)-3-methylvaleric acid
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KEGG COMPOUND
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D-Isoleucine
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KEGG COMPOUND
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D-ISOLEUCINE
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PDBeChem
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DIL
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PDBeChem
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1721793
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Reaxys Registry Number
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Reaxys
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278733
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Gmelin Registry Number
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Gmelin
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319-78-8
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CAS Registry Number
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ChemIDplus
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Akita H, Imaizumi Y, Suzuki H, Doi K, Ohshima T (2014)
Spectrophotometric assay of D-isoleucine using an artificially created D-amino acid dehydrogenase.
Biotechnology letters 36, 2245-2248 [PubMed:24966047]
[show Abstract]
D-isoleucine (D-Ile) can be assayed using chiral chromatography but the availability of that method is limited by the necessity for special expertise and expensive equipment. We therefore developed a simple and specific colorimetric assay system for D-Ile determination using an artificially created NADP(+)-dependent D-amino acid dehydrogenase (DAADH). The system consists of two reaction steps: the first is the quantitative conversion of D-Ile to (3R)-2-oxo-3-methyl valerate by DAADH in which NADP(+) is converted to NADPH, while the second is chemical conversion of NADPH to reduced water-soluble Tetrazolium-3 via a redox mediator. D-Ile was determined from 1 to 50 µM, and the assay was unaffected by the presence of any of three other isomers (100 µM), alcohol and organic acids. | Dörries K, Lalk M (2013)
Metabolic footprint analysis uncovers strain specific overflow metabolism and D-isoleucine production of Staphylococcus aureus COL and HG001.
PloS one 8, e81500 [PubMed:24312553]
[show Abstract]
During infection processes, Staphylococcus aureus is able to survive within the host and to invade tissues and cells. For studying the interaction between the pathogenic bacterium and the host cell, the bacterial growth behaviour and its metabolic adaptation to the host cell environment provides first basic information. In the present study, we therefore cultivated S. aureus COL and HG001 in the eukaryotic cell culture medium RPMI 1640 and analyzed the extracellular metabolic uptake and secretion patterns of both commonly used laboratory strains. Extracellular accumulation of D-isoleucine was detected starting during exponential growth of COL and HG001 in RPMI medium. This non-canonical D-amino acid is known to play a regulatory role in adaptation processes. Moreover, individual uptake of glucose, accumulation of acetate, further overflow metabolites, and intermediates of the branched-chain amino acid metabolism constitute unique metabolic footprints. Altogether these time-resolved footprint analyses give first metabolic insights into staphylococcal growth behaviour in a culture medium used for infection related studies. | Holmberg S, Petersen JG (1988)
Regulation of isoleucine-valine biosynthesis in Saccharomyces cerevisiae.
Current genetics 13, 207-217 [PubMed:3289762]
[show Abstract]
The threonine deaminase gene (ILV1) of Saccharomyces cerevisiae has been designated "multifunctional" since Bollon (1974) indicated its involvement both in the catalysis of the first step in isoleucine biosynthesis and in the regulation of the isoleucine-valine pathway. Its role in regulation is characterized by a decrease in the activity of the five isoleucine-valine enzymes when cells are grown in the presence of the three branched-chain amino acids, isoleucine, valine and leucine (multivalent repression). We have demonstrated that the regulation of AHA reductoisomerase (encoded by ILV5) and branched-chain amino acid transaminase is unaffected by the deletion of ILV1, subsequently revealing that the two enzymes can be regulated in the absence of threonine deaminase. Both threonine deaminase activity and ILV1 mRNA levels increase in mutants (gcd2 and gcd3) having constitutively depressed levels of enzymes under the general control of amino acid biosynthesis, as well as in response to starvation for tryptophan and branched-chain amino acid imbalance. Thus, the ILV1 gene is under general amino acid control, as is the case for both the ILV5 and the transaminase gene. Multivalent repression of reductoisomerase and transaminase can be observed in mutants defective in general control (gcn and gcd), whereas this is not the case for threonine deaminase. Our analysis suggests that repression effected by general control is not complete in minimal medium. Amino acid dependent regulation of threonine deaminase is only through general control, while the branched-chain amino acid repression of AHA reducto isomerase and the transaminase is caused both by general control and an amino acid-specific regulation. | Yajima T, Mason K, Katz E (1976)
Biogenetic origin of the D-isoleucine and N-methyl-L-alloisoleucine residues in the actinomycins.
Antimicrobial agents and chemotherapy 9, 224-232 [PubMed:57739]
[show Abstract]
Studies with (14)C-labeled isoleucine stereisomers have established that l-alloisoleucine, d-alloisoleucine, and d-isoleucine may function as precursors for the biogenesis of d-isoleucine and N-methyl-l-alloisoleucine residues in actinomycin. l-[(14)C]isoleucine appears to be employed chiefly for d-alloisoleucine (and N-methylisoleucine [?] formation); however, its role in the biosynthesis of d-isoleucine and N-methylalloisoleucine remains unclear. The potential pathway of biosynthesis of d-isoleucine and N-methyl-l-isoleucine is discussed. | Conrad RS, Massey LK, Sokatch JR (1974)
D- and L-isoleucine metabolism and regulation of their pathways in Pseudomonas putida.
Journal of bacteriology 118, 103-111 [PubMed:4150713]
[show Abstract]
Pseudomonas putida oxidized isoleucine to acetyl-coenzyme A (CoA) and propionyl-CoA by a pathway which involved deamination of d-isoleucine by oxidation and l-isoleucine by transamination, oxidative decarboxylation, and beta oxidation at the ethyl side chain. At least three separate inductive events were required to form all of the enzymes of the pathway: d-amino acid dehydrogenase was induced during growth in the presence of d-isoleucine; branched-chain keto dehydrogenase was induced during growth on 2-keto-3-methylvalerate and enzymes specific for isoleucine metabolism; tiglyl-CoA hydrase and 2-methyl-3-hydroxybutyryl-CoA dehydrogenase were induced by growth on isoleucine, 2-keto-3-methylvalerate, 2-methylbutyrate, or tiglate. Tiglyl-CoA hydrase and 2-methyl-3-hydroxybutyryl-CoA dehydrogenase were purified simultaneously by several enzyme concentration procedures, but were separated by isoelectric focusing. Isoelectric points, pH optima, substrate specificity, and requirements for enzyme action were determined for both enzymes. Evidence was obtained that the dehydrogenase catalyzed the oxidation of 2-methyl-3-hydroxybutyryl-CoA to 2-methylacetoacetyl-CoA. 2-Methyl-3-hydroxybutyryl-CoA dehydrogenase catalyzed the oxidation of 3-hydroxybutyryl-CoA, but l-3-hydroxyacyl-CoA dehydrogenase from pig heart did not catalyze the oxidation of 2-methyl-3-hydroxybutyryl-CoA; therefore, they appeared to be different dehydrogenases. Furthermore, growth on tiglate resulted in the induction of tiglyl-CoA hydrase and 2-methyl-3-hydroxybutyryl-CoA dehydrogenase, but these two enzymes were not induced during growth on crotonate or 3-hydroxybutyrate. |
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