TY - JOUR
T1 - Characterization of TioQ, a type II thioesterase from the thiocoraline biosynthetic cluster
AU - Mady, Ahmed S.A.
AU - Zolova, Olga E.
AU - Millán, María Álvarez San
AU - Villamizar, Germán
AU - Calle, Fernando De La
AU - Lombó, Felipe
AU - Garneau-Tsodikova, Sylvie
PY - 2011/6/1
Y1 - 2011/6/1
N2 - An antitumor agent thiocoraline is a thiodepsipeptide marine product derived from two Micromonospora sp. strains that inhibits protein synthesis by binding of its key 3-hydroxyquinaldic acid (3HQA) chromophores to duplex DNA. There are at least two potential pathways via which the 3HQA moiety could be biosynthesized from l-Trp. By biochemical characterization and by preparation of knockouts of an adenylation-thiolation enzyme, TioK, and of two type II thioesterases, TioP and TioQ, found in the thiocoraline biosynthetic gene cluster, we gained valuable insight into the pathway followed for the production of 3HQA.
AB - An antitumor agent thiocoraline is a thiodepsipeptide marine product derived from two Micromonospora sp. strains that inhibits protein synthesis by binding of its key 3-hydroxyquinaldic acid (3HQA) chromophores to duplex DNA. There are at least two potential pathways via which the 3HQA moiety could be biosynthesized from l-Trp. By biochemical characterization and by preparation of knockouts of an adenylation-thiolation enzyme, TioK, and of two type II thioesterases, TioP and TioQ, found in the thiocoraline biosynthetic gene cluster, we gained valuable insight into the pathway followed for the production of 3HQA.
UR - http://www.scopus.com/inward/record.url?scp=79956150138&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=79956150138&partnerID=8YFLogxK
U2 - 10.1039/c1mb05044c
DO - 10.1039/c1mb05044c
M3 - Article
C2 - 21483938
AN - SCOPUS:79956150138
SN - 1742-206X
VL - 7
SP - 1999
EP - 2011
JO - Molecular BioSystems
JF - Molecular BioSystems
IS - 6
ER -
