Discovery of 3-formyl-tyrosine metabolites from Pseudoalteromonas tunicata through heterologous expression.
Genome mining and identification of natural product gene clusters typically relies on the presence of canonical nonribosomal polypeptide synthetase (NRPS) or polyketide synthase (PKS) domains. Recently, other condensation enzymes, such as the ATP-grasp ligases, have been recognized as important players in natural product biosynthesis. In this study, sequence based searching for homologues of DdaF, the ATP-grasp amide ligase from dapdiamide biosynthesis, led to the identification of a previously unannotated biosynthetic gene cluster in Pseudoalteromonas tunicata. Heterologous expression of the cluster in Escherichia coli allowed for the production and structure determination of two new 3-formyl tyrosine metabolites.
Blasiak
Leah C
LC
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Ave, Boston, Massachusetts 02115, USA.
Clardy
Jon
J
D008968:Molecular Conformation; D031161:Pseudoalteromonas / Q000737:chemistry / Q000378:metabolism*; D013237:Stereoisomerism; D014443:Tyrosine / Q000031:analogs & derivatives / Q000737:chemistry / Q000378:metabolism*
D014443:Tyrosine