title: A domain of RubC1 of rubradirin biosynthesis can functionally replace MbtH-like proteins in tyrosine adenylation.
abstract: Master of your domain: A domain of the bifunctional enzyme RubC1 catalyzes the adenylation of tyrosine. This domain can be activated not only by MbtH-like proteins but also by another domain of RubC1 that has no similarity to MbtH-like proteins.
authors.affiliation: Pharmazeutisches Institut, Universität Tübingen, Auf der Morgenstelle 8, 72076 Tübingen.
authors.forename: Björn
authors.initials: B
authors.lastname: Boll
authors.forename: Lutz
authors.initials: L
authors.lastname: Heide
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D009285:Naphthoquinones / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D014443:Tyrosine / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D009285:Naphthoquinones; D014443:Tyrosine; C002857:rubradirin