Protein Family Models

This entry represents the N-terminal domain of enterochelin esterase. The activity of the enzyme has been characterised [1, 2]. Fes catalyses the hydrolysis of the 2,3-dihydroxy-N- benzoyl-L-serine trimer, enterochelin, forming 2,3- dihydroxybenzoylserine. It also catalyses hydrolysis of free enterobactin and ferric enterobactin. Upon hydrolysis of ferric enterobactin by Fes, released iron is probably reduced by a second enzyme. Enterochelin esterase represents a family of non-peptidase homologues belonging to the MEROPS peptidase family S9, clan SC. [1]. 1534808. Overexpression and purification of ferric enterobactin esterase from Escherichia coli. Demonstration of enzymatic hydrolysis of enterobactin and its iron complex. Brickman TJ, McIntosh MA;. J Biol Chem. 1992;267:12350-12355. [2]. 16076215. In vitro characterization of salmochelin and enterobactin trilactone hydrolases IroD, IroE, and Fes. Lin H, Fischbach MA, Liu DR, Walsh CT;. J Am Chem Soc. 2005;127:11075-11084. (from Pfam)

Date:

2024-10-16

Members of this family alpha/beta hydrolase-fold proteins. Known members include hydrolases such as S-formylglutathione hydrolase (called esterase D in human) and the three paralogous mycolyltransferases of the Ag85 complex in Mycobacterium tuberculosis.

Date:

2024-08-14

alpha/beta hydrolase family protein catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

Date:

2024-04-29