| Description | This entry represents a structural motif found at the C-terminal of lactate dehydrogenase ( )and malate dehydrogenases ( ), as well as at the C-terminal of family 4 glycoside hydrolases ( ). These domains have an unusual fold consisting of segregated α-helical and β-sheet regions, although they contain predominantly anti-parallel β-sheets [ , , ].L-lactate dehydrogenases are metabolic enzymes that catalyse the conversion of L-lactate to pyruvate, the last step in anaerobic glycolysis. L-lactate dehydrogenase is also found as a lens crystallin in bird and crocodile eyes. Malate dehydrogenases catalyse the interconversion of malate to oxaloacetate. The enzyme participates in the citric acid cycle.O-Glycosyl hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ , ]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in 'clans'. Glycoside hydrolase family 4 comprises enzymes with several known activities; 6-phospho-beta-glucosidase ( ); 6-phospho-alpha-glucosidase ( ); alpha-galactosidase ( ). | Name | Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal |
| Short Name | Lactate_DH/Glyco_Ohase_4_C | Type | Homologous_superfamily |
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