Literature summary for 2.4.1.170 extracted from

Koirala, N.; Pandey, R.P.; Thang, D.V.; Jung, H.J.; Sohng, J.K.
Glycosylation and subsequent malonylation of isoflavonoids in E. coli: strain development, production and insights into future metabolic perspectives (2014), J. Ind. Microbiol. Biotechnol., 41, 1647-1658.

Search for more literature for 2.4.1.170

Application

Application	Comment	Organism
drug development	isoflavonoids and their glycosides may prove useful as anticancer drugs with added advantage of increased solubility, stability and bioavailability. Among the six compounds tested, genistein most effectively inhibits the growth of B16F10 and AGS cells, with IC50 values of 0.0077 mM and 0.0398 mM, respectively. Unlike derivatives of genistein (genistin and biochanin A), the glycosylated and methylated forms of daidzein (daidzin and formononetin) exhibit more effective growth inhibition than aglycon, daidzein	Glycine max

Cloned(Commentary)

Cloned (Comment)	Organism
gene GmIF7GT, recombinant functional expression in Escherichia coli strain BL21(DE3), coexpression with acyl-CoA carboxylase alpha and beta subunits, biotin ligase, and acetyl-CoA synthetase from Nocardia farcinia for subsequent malonylization of the reaction product of GmIF7GT-encoded isoflavone 7-O-glucosyltransferase. The isoflavonoids are glycosylated at position 7 by 7-O-glycosyltranferase and are further malonylated at position 6' of glucose by malonyl-CoA:isoflavone 7-O-glucoside-6'-O-malonyltransferase both from Glycine max	Glycine max

Cloned (Comment)

Organism

gene GmIF7GT, recombinant functional expression in Escherichia coli strain BL21(DE3), coexpression with acyl-CoA carboxylase alpha and beta subunits, biotin ligase, and acetyl-CoA synthetase from Nocardia farcinia for subsequent malonylization of the reaction product of GmIF7GT-encoded isoflavone 7-O-glucosyltransferase. The isoflavonoids are glycosylated at position 7 by 7-O-glycosyltranferase and are further malonylated at position 6' of glucose by malonyl-CoA:isoflavone 7-O-glucoside-6'-O-malonyltransferase both from Glycine max

Glycine max

Protein Variants

Protein Variants	Comment	Organism
additional information	cell engineering by GmIF7GT enzyme coexpression with acyl-CoA carboxylase alpha and beta subunits, biotin ligase, and acetyl-CoA synthetase from Nocardia farcinia for subsequent malonylization of the reaction product of GmIF7GT-encoded isoflavone 7-O-glucosyltransferase. The isoflavonoids are glycosylated at position 7 by 7-O-glycosyltranferase and are further malonylated at position 6' of glucose by malonyl-CoA:isoflavone 7-O-glucoside-6'-O-malonyltransferase both from Glycine max, Scale up for production using a fermentor	Glycine max

Organism

Organism	UniProt	Comment	Textmining
Glycine max	A6BM07	or Glycine hispida, gene GmIF7GT	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
UDP-glucose + biochanin A	-	Glycine max	UDP + biochanin A 7-O-beta-D-glucoside	-	?
UDP-glucose + daidzein	-	Glycine max	UDP + daidzein 7-O-beta-D-glucoside	-	?
UDP-glucose + genistein	-	Glycine max	UDP + genistein 7-O-beta-D-glucoside	-	?