Literature summary for 1.2.1.104 extracted from

Chandrasekhar, K.; Arjunan, P.; Sax, M.; Nemeria, N.; Jordan, F.; Furey, W.
Active-site changes in the pyruvate dehydrogenase multienzyme complex E1 apoenzyme component from Escherichia coli observed at 2.32 A resolution (2006), Acta Crystallogr. Sect. D, 62, 1382-1386 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
component E1 without cofactors thiamine diphosphate and Mg2+, at 2.32 A resolution. Water molecules may form a hydrogen-bonded linkage between residues Glu571 and Val192, which normally make conserved interactions with the thiamine diphosphate cofactor. A histidine side chain that normally forms hydrogen bonds to thiamine diphosphate is disordered in its absence and partially occupies two sites. No disorder/order loop transformations are evident in the apo-E1 component relative to the holo-E1 enzyme	Escherichia coli

Crystallization (Comment)

Organism

component E1 without cofactors thiamine diphosphate and Mg2+, at 2.32 A resolution. Water molecules may form a hydrogen-bonded linkage between residues Glu571 and Val192, which normally make conserved interactions with the thiamine diphosphate cofactor. A histidine side chain that normally forms hydrogen bonds to thiamine diphosphate is disordered in its absence and partially occupies two sites. No disorder/order loop transformations are evident in the apo-E1 component relative to the holo-E1 enzyme

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0AFG8	E1 component AceE, cf. EC 1.2.4.1	-

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Release 2023.1 (January 2023)