CHEBI:85306 - D-alloisoleucine zwitterion

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ChEBI Name D-alloisoleucine zwitterion ChEBI ID CHEBI:85306 ChEBI ASCII Name D-alloisoleucine zwitterion Definition A D-α-amino acid zwitterion resulting from a transfer of a proton from the carboxy group to the amino group of D-alloisoleucine; major species at pH 7.3. Stars This entity has been manually annotated by the ChEBI Team. Submitter Kristian Axelsen Supplier Information ChemicalBook:CB5755462, eMolecules:476205, ZINC000000388314 Download Molfile XML SDF Find compounds which contain this structure Find compounds which resemble this structure Take structure to the Advanced Search Formula C6H13NO2 Net Charge 0 Average Mass 131.17290 Monoisotopic Mass 131.09463 InChI InChI=1S/C6H13NO2/c1-3-4(2)5(7)6(8)9/h4-5H,3,7H2,1-2H3,(H,8,9)/t4-,5+/m0/s1 InChIKey AGPKZVBTJJNPAG-CRCLSJGQSA-N SMILES CC[C@H](C)[C@@H]([NH3+])C([O-])=O ChEBI Ontology Outgoing D-alloisoleucine zwitterion (CHEBI:85306) is a D-α-amino acid zwitterion (CHEBI:59871) D-alloisoleucine zwitterion (CHEBI:85306) is enantiomer of L-alloisoleucine zwitterion (CHEBI:85338) D-alloisoleucine zwitterion (CHEBI:85306) is tautomer of D-alloisoleucine (CHEBI:20899) Incoming L-alloisoleucine zwitterion (CHEBI:85338) is enantiomer of D-alloisoleucine zwitterion (CHEBI:85306) D-alloisoleucine (CHEBI:20899) is tautomer of D-alloisoleucine zwitterion (CHEBI:85306) IUPAC Name (2R,3S)-2-azaniumyl-3-methylpentanoate Synonym Source D-allo-isoleucine UniProt Manual Xref Database CPD-17659 MetaCyc View more database links Citation Mutaguchi Y, Ohmori T, Wakamatsu T, Doi K, Ohshima T (2013) Identification, purification, and characterization of a novel amino acid racemase, isoleucine 2-epimerase, from Lactobacillus species. Journal of bacteriology 195, 5207-5215 (Source: SUBMITTER) [PubMed:24039265] [show Abstract] Accumulation of d-leucine, d-allo-isoleucine, and d-valine was observed in the growth medium of a lactic acid bacterium, Lactobacillus otakiensis JCM 15040, and the racemase responsible was purified from the cells and identified. The N-terminal amino acid sequence of the purified enzyme was GKLDKASKLI, which is consistent with that of a putative γ-aminobutyrate aminotransferase from Lactobacillus buchneri. The putative γ-aminobutyrate aminotransferase gene from L. buchneri JCM 1115 was expressed in recombinant Escherichia coli and then purified to homogeneity. The enzyme catalyzed the racemization of a broad spectrum of nonpolar amino acids. In particular, it catalyzed at high rates the epimerization of l-isoleucine to d-allo-isoleucine and d-allo-isoleucine to l-isoleucine. In contrast, the enzyme showed no γ-aminobutyrate aminotransferase activity. The relative molecular masses of the subunit and native enzyme were estimated to be about 49 kDa and 200 kDa, respectively, indicating that the enzyme was composed of four subunits of equal molecular masses. The Km and Vmax values of the enzyme for l-isoleucine were 5.00 mM and 153 μmol·min(-1)·mg(-1), respectively, and those for d-allo-isoleucine were 13.2 mM and 286 μmol·min(-1)·mg(-1), respectively. Hydroxylamine and other inhibitors of pyridoxal 5'-phosphate-dependent enzymes completely blocked the enzyme activity, indicating the enzyme requires pyridoxal 5'-phosphate as a coenzyme. This is the first evidence of an amino acid racemase that specifically catalyzes racemization of nonpolar amino acids at the C-2 position. Last Modified 13 March 2017