The structure of Mesorhizobium loti arylamine N-acetyltransferase 1 (NAT1) in complex with coenzyme A provides further understanding of the mode of binding of the cofactor in this family of enzymes.

The structure of M. extorquens malyl-CoA lyase is reported, along with a detailed analysis of the domain motions involved in regulating its enzymatic activity.

Crystallographic fragment-binding studies of the Mycobacterium tuberculosis trifunctional enzyme have resulted in 121 binding events of 16 out of 226 investigated fragments, suggesting functional sites with respect to substrate binding and substrate channeling.

Mycobacterium tuberculosis MenB, or 1, 4-dihydroxynaphthoyl coenzyme A synthase, is found to undergo induced-fit conformational changes that play an important role in substrate recognition and catalytic mechanism.

Serine palmitoyltransferase (SPT) is the rate-limiting key enzyme in the sphingolipid biosynthetic pathway. Here, the structure of SPT from S. multivorum complexed with tris(hydroxymethyl)aminomethane is reported at 1.65 Å resolution, which is an improvement on the previously reported structure at 2.3 Å resolution.

Biotin protein ligase from Leishmania major in complex with biotinyl-5′-AMP or biotin, crystallizes as a unique dimer, formed by cross-handshake interactions of its C-terminal domain.

The structure of barley agmatine coumaroyltransferase, a member of the BAHD acyltransferase superfamily, was elucidated. This is the first report of the structure of an N-acyltransferase from the BAHD superfamily.

Stable analogs of acetyl-CoA are needed to support structure–function studies of acetyltransferase enzymes. Here, the structures of two enzymes in the presence of an acetyl-CoA analog in which the thioester is replaced by an ester are reported.

Structural characterization of MAB_4123, a putative two-component flavin-dependent monooxygenase from the human pathogen Mycobacterium abscessus, suggests a role in the catabolic pathway of organosulfur compounds.

AjiA1 is an adenylate-forming enzyme (AFE) family member that catalyzes the condensation of two molecules of 3-hydroxyanthranilic acid using ATP as a co-substrate. The structure of AjiA1 in its apo form was solved and revealed key conformational changes, including an unusual loop swapping, suggesting that it should be classified into a new AFE subgroup.