Literature summary for 2.3.1.94 extracted from

Ostrowski, M.P.; Cane, D.E.; Khosla, C.
Recognition of acyl carrier proteins by ketoreductases in assembly line polyketide synthases (2016), J. Antibiot., 69, 507-510 .

Search for more literature for 2.3.1.94

Organism

Organism	UniProt	Comment	Textmining
Saccharopolyspora erythraea	Q03131 and Q03132 and Q03133	Q03131 i.e. modules 1 and 2, Q03132 i.e. modules 3 and 4, Q03133 i.e. modules 5 and 6	-

General Information

General Information	Comment	Organism
physiological function	ketoreductases from DEBS modules 2 and 5 display little preference for oxidation of substrates tethered to their cognate ACP domains over those attached to the other ACP domains tested. The ketoreductase from DEBS module 1 shows an about 10-50fold preference for substrate attached to its native ACP domain, whereas the ketoreductase from DEBS module 6 displays an about 10fold preference for the ACP from DEBS module 5	Saccharopolyspora erythraea

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)