InChI=1S/C16H24N2O15P2/c1- 6- 4- 18(16(24) 17- 14(6) 23) 10- 3- 8(19) 9(31- 10) 5- 29- 34(25,26) 33- 35(27,28) 32- 15- 13(22) 12(21) 11(20) 7(2) 30- 15/h4,7- 10,12- 13,15,19,21- 22H,3,5H2,1- 2H3,(H,25,26) (H,27,28) (H,17,23,24) /p- 2/t7- ,8- ,9+,10+,12+,13+,15+/m0/s1 |
PSXWNITXWWECNY-LPVGZGSHSA-L |
C[C@@H] 1O[C@H] (OP([O- ] ) (=O) OP([O- ] ) (=O) OC[C@H] 2O[C@H] (C[C@@H] 2O) n2cc(C) c(=O) [nH] c2=O) [C@H] (O) [C@H] (O) C1=O |
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thymidine 5'-[3-(6-deoxy-β-L-lyxo-hexopyranosyl-4-ulose) diphosphate]
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dTDP-4-dehydro-β-L-rhamnose
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UniProt
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dTDP-6-deoxy-β-L-lyxo-hex-4-ulose(2−)
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ChEBI
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dTDP-L-lyxo-hexulose
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SUBMITTER
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Hirao Y, Mihara Y, Kira I, Abe I, Yokozeki K (2013) Enzymatic production of L-alanyl-L-glutamine by recombinant E. coli expressing α-amino acid ester acyltransferase from Sphingobacterium siyangensis. Bioscience, biotechnology, and biochemistry 77, 618-623 (Source: SUBMITTER) [PubMed:23470770] [show Abstract] An enzymatic production method for synthesizing L-alanyl-L-glutamine (Ala-Gln) from L-alanine methyl ester hydrochloride (AlaOMe) and L-glutamine (Gln) was developed in this study. The cultivation conditions for an Escherichia coli strain overexpressing α-amino acid ester acyltransferase from Sphingobacterium siyangensis AJ 2458 (SAET) and reaction conditions for Ala-Gln production were optimized. A high cell density culture broth prepared by fed-batch cultivation showed 440 units/mL of Ala-Gln-producing activity. In addition, an Ala-Gln-producing reaction using intact E. coli cells overexpressing SAET under optimum conditions was conducted. A total Ala-Gln yield of 69.7 g/L was produced in 40 min. The molar yield was 67% against both AlaOMe and Gln. |
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