4-Hydroxy-2-oxoglutarate aldolase () (KHG-aldolase) catalyzes the interconversion of 4-hydroxy-2-oxoglutarate into pyruvate and glyoxylate. Phospho-2-dehydro-3-deoxygluconate aldolase () (KDPG-aldolase) catalyzes the interconversion of 6-phospho-2-dehydro-3-deoxy-D-gluconate into pyruvate and glyceraldehyde 3-phosphate. E. coli Eda is a KDPG-aldolase that has also been found to have a role in the degradation of 2-keto-4-hydroxyglutarate (KHG) to pyruvate and glyoxylate []. In fact, KHG-aldolase and Eda are the same enzyme [].This family consists of KHG/KDPG aldolases, and also includes 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) aldolase. KDPGal-aldolase catalyzes an identical reaction to KDPG, differing in substrate specificity in only the configuration of a single stereocentre [].
TNFRSF27 (also known as ectodysplasin-A2 receptor (EDA2R), X-linked ectodermal dysplasia receptor (XEDAR), EDAA2R, EDA-A2R) is a member of the TNFR superfamily that is recognised by ectodysplasin-A2 (EDA-A2), which is generated by alternative splicing of the EDA receptor (EDAR) ligand EDA-A1 []. It is highly expressed during embryonic development and binds to ectodysplasin-A2 (EDA-A2), playing a crucial role in the p53-signaling pathway. EDA2R is a direct p53 target that is frequently down-regulated in colorectal cancer tissues due to its epigenetic alterations or through the p53 gene mutations [, ]. Mutations in the EDA-A2/XEDAR signaling give rise to ectodermal dysplasia, characterized by loss of hair, sweat glands, and teeth []. A non-synonymous SNP on EDA2R, along with genetic variants in human androgen receptor is associated with androgenetic alopecia (AGA) [].This entry represents the N-terminal domain of TNFRSF27/XEDAR. TNF-receptors are modular proteins. The N-terminal extracellular part contains a cysteine-rich region responsible for ligand-binding. This region is composed of small modules of about 40 residues containing 6 conserved cysteines; the number and type of modules can vary in different members of the family [, , ].