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B6db activities: lipk

Description L-threonine--uridine -5-aldehyde transaldolase (2.2.1.-)
Catalyzed reaction Uridine-5′-aldehyde + L-threonine = 5'-C-glycyluridine + acetaldehyde
Cofactor Pyridoxal-phosphate
LipK is an enzyme responsible for the CC bond-forming event during GlyU biosynthesis as an L-threonine:uridine-5′-aldehyde transaldolase.
The enzyme from Streptomyces sp. SANK 60405 has no activity with alternative amino acids such as glycine or serine as aldol donors, and acetaldehyde is a co-product.
Organisms -Eubacteria


lipk (0)
Links Enzyme (activities) lipk
BRENDA (activities) lipk
KEGG (pathways) lipk
PLPMDB (PLP mutants) lipk
 Cui Z, Liu X, Overbay J, Cai W, Wang X, Lemke A, Wiegmann D, Niro G, Thorson JS, Ducho C, Van Lanen SG (2018) Enzymatic Synthesis of the Ribosylated Glycyl-Uridine Disaccharide Core of Peptidyl Nucleoside Antibiotics J Org Chem 83 7239-7249.

 Huang Y, Liu X, Cui Z, Wiegmann D, Niro G, Ducho C, Song Y, Yang Z, Van Lanen SG. (2018) Pyridoxal-5'-phosphate as an oxygenase cofactor: Discovery of a carboxamide-forming, alfa-amino acid monooxygenase-decarboxylase. Proc Natl Acad Sci U S A. 115 974-979.

 Funabashi M, Baba S, Takatsu T, Kizuka M, Ohata Y, Tanaka M, Nonaka K, Spork AP, Ducho C, Chen WC, Van Lanen SG (2013) Structure-based gene targeting discovery of sphaerimicin, a bacterial translocase I inhibitor Angew Chem Int Ed Engl 52 11607-11.

 Barnard-Britson, S,; Chi, X.; Nonaka, K.; Spork, A.P.; Tibrewal, N.; Goswami, A.; Pahari, P.; Ducho, C.; Rohr, J.; Van Lanen, S.G. (2012) Amalgamation of Nucleosides and Amino Acids in Antibiotic Biosynthesis: Discovery of an L-Threonine:Uridine-5'-Aldehyde Transaldolase J Am Chem Soc 134 18514-7.

Articles on lipk
last changed 2019/12/28 20:21

B6db activities