Literature summary for 1.2.4.1 extracted from

Hezaveh, S.; Zeng, A.P.; Jandt, U.
Full enzyme complex simulation interactions in human pyruvate dehydrogenase complex (2018), J. Chem. Inf. Model., 58, 362-369 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
full and dynamic structural model of full human pyruvate dehydrogenase complex, including binding of the linking arms to the surrounding E1 (pyruvate decarboxylase) and E3 (dihydrolipoamide dehydrogenase) enzymes via their binding domains with variable stoichiometries. An optimalsetting of approximately 30 copies of E1 ensures stability of the surrounding E1 and E3 clouds. Decreasing the number of E1s increases the flexibility of the now nonoccupied arms. Their flexibility depends on the presence of other E1s and E3s in the vicinity, even if they are associated with other arms. As one consequence, the radius of gyration decreases with decreasing number of E1s	Homo sapiens

Crystallization (Comment)

Organism

full and dynamic structural model of full human pyruvate dehydrogenase complex, including binding of the linking arms to the surrounding E1 (pyruvate decarboxylase) and E3 (dihydrolipoamide dehydrogenase) enzymes via their binding domains with variable stoichiometries. An optimalsetting of approximately 30 copies of E1 ensures stability of the surrounding E1 and E3 clouds. Decreasing the number of E1s increases the flexibility of the now nonoccupied arms. Their flexibility depends on the presence of other E1s and E3s in the vicinity, even if they are associated with other arms. As one consequence, the radius of gyration decreases with decreasing number of E1s

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

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Release 2023.1 (January 2023)