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EC Number	Subunits	Commentary	Reference
6.3.2.1	?	x * 18000, SDS-PAGE in presence of 2-mercaptoethanol	-, 977, 980
6.3.2.1	?	x * 33900, deduced from nucleotide sequence	649671
6.3.2.1	?	x * 43000, SDS-PAGE	653240
6.3.2.1	dimer	-	674714
6.3.2.1	dimer	2 * 30000, SDS-PAGE	653927
6.3.2.1	dimer	2 * 31611, mass spectroscopy, crystallization	653802
6.3.2.1	dimer	2 * 32677, deduced from nucleotide sequence	650029
6.3.2.1	dimer	2 * 33000, SDS-PAGE	650029
6.3.2.1	dimer	2 * 34000, SDS-PAGE	649671
6.3.2.1	dimer	molecular dynamics simulations show that the functional dynamics of the enzyme are dominated by motions of a flexible gate loop in the N-terminal domain and of the C-terminal domain. The gate loop motions dominate in Mycobacterium tuberculosis pantothenate synthetase while the C-terminal domain motion dominates in Escherichia coli pantothenate synthetase. Simulations also show that the correlated motions of the domains are severely compromised in the monomeric forms	716880

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Release 2023.1 (January 2023)