Protein Family Models

Fumarase C catalyses the stereo-specific interconversion of fumarate to L-malate as part of the Kreb's cycle. The full-length protein forms a tetramer with visible globular shape. FumaraseC_C is the C-terminal 65 residues referred to as domain 3. The core of the molecule consists of a bundle of 20 alpha-helices from the five-helix bundle of domain 2. The projections from the core of the tetramer are generated from domains 1 and 3 of each subunit [1]. FumaraseC_C does not appear to be part of either the active site or the activation site but is helical in structure forming a little bundle. [1]. 8909293. Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli. Weaver T, Banaszak L;. Biochemistry. 1996;35:13955-13965. (from Pfam)

Date:

2024-10-16

Members of this family include fumarate hydratase, L-aspartate ammonia-lyase, argininosuccinate lyase, and adenylosuccinate lyase. All are classified as lyases, meaning these enzymes break a bond by an eliminating reaction that does not involve hydrolysis or oxidation.

Date:

2024-08-14

Catalyzes the formation of fumarate from aspartate

Date:

2020-10-26

Catalyzes the formation of fumarate from aspartate

Date:

2021-11-04

This enzyme, aspartate ammonia-lyase, shows local homology to a number of other lyases, as modeled by Pfam HMM PF00206. Fumarate hydratase scores as high as 570 bits against this model.

Gene:

aspA

Date:

2021-04-27