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racemic norleucine methyl ester  (Chem Impex International)


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    Chem Impex International racemic norleucine methyl ester
    Racemic Norleucine Methyl Ester, supplied by Chem Impex International, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/02004/DL-Norleucine/10__1002_slash_bkcs__11694-75-15-19
    Average 95 stars, based on 1 article reviews
    racemic norleucine methyl ester - by Bioz Stars, 2026-09
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    Article Title: Determination of Chemical and Enantiomeric Purity of α‐Amino Acids and their Methyl Esters as N‐Fluorenylmethoxycarbonyl Derivatives Using Amylose‐derived Chiral Stationary Phases
    Article Snippet: Liquid chromatographic enantiomer separation and simultaneous determination of chemical and enantiomeric purity of α-amino acids and their methyl esters as N-fluorenylmethoxycarbonyl (FMOC) derivatives was performed on three covalently bonded type chiral stationary phases (CSPs) derived from amylose derivatives.. The enantiomer separation of α-amino acid esters as N-FMOC derivatives was better than that of the corresponding acids, especially for CSP 1 and 2.. Chemical impurities as the corresponding racemic acids present in several commercially available racemic amino acid methyl esters were observed to be 0.49–17.50%.



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    Predicted conserved domains and putative functions of proteins encoded by genes identified in a 12-kb genomic fragment of Acinetobacter sp. O153

    Journal: Applied and Environmental Microbiology

    Article Title: Indole Biodegradation in Acinetobacter sp. Strain O153: Genetic and Biochemical Characterization

    doi: 10.1128/AEM.01453-17

    Figure Lengend Snippet: Predicted conserved domains and putative functions of proteins encoded by genes identified in a 12-kb genomic fragment of Acinetobacter sp. O153

    Article Snippet: Identities (percent) of amino acid sequences between Iif proteins of strain O153 and homologs are indicated under the corresponding ORFs. table ft1 table-wrap mode="anchored" t5 TABLE 1 caption a7 Protein Conserved domain (identifier) E value Closest homolog with known function Protein a GenBank accession no. or identifier Function Identity (%) Reference IifA α/β hydrolase (COG0412) 2.3e−53 ClcD from P. knackmussii B13 AAB71539.1 Dienelactone hydrolase 34 66 SnoaL-like polyketide cyclase (pfam07366) 0.04 IifB Short-chain dehydrogenase (cd05233) 1.2e−56 FabG from V. cholerae N16961 VC2021 Reduction of β-ketoacyl-ACP to 3-hydroxyacyl-ACP 33 67 IifC IifC from A. baumannii ATCC 19606 F911_02004 Monooxygenase 82 23 IifD Flavin reductase (COG1853) 6.8e−40 IifD from A. baumannii ATCC 19606 F911_02003 Flavin reductase 81 23 IifE MetA-pathway of phenol degradation (cl01768) 1.3e−57 Pput2725 from P. putida F1 4RL8 Outer membrane channel of unknown function 21 68 IifR AraC-binding-like domain (pfam14525) 4e−39 IifR from A. baumannii ATCC 19606 F911_02001 Transcriptional regulator 74 23 AntA Rieske non-heme iron oxygenase (cd03469) 9e−46 AntA from Acinetobacter sp. ADP1 AAC34813.1 Oxygenase component of anthranilate dioxygenase 93 31 C-terminal catalytic domain of the oxygenase alpha subunit (cd08879) 9e−83 AntB Ring hydroxylating beta subunit (cd00667) 2e−51 AntB from Acinetobacter sp. ADP1 AAC34814.1 Oxygenase component of anthranilate dioxygenase 94 31 AntC Benzoate dioxygenase reductase FAD/NAD binding domain (cd06209) 3e−107 AntC from Acinetobacter sp. ADP1 AAC34815.1 Reductase component of anthranilate dioxygenase 87 31 2Fe-2S cluster (cd00207) 3e−21 Open in a separate window a P. knackmussii , Pseudomonas knackmussii ; V. cholerae , Vibrio cholerae .

    Techniques: Membrane, Binding Assay