Literature summary extracted from

Nakai, T.; Nakagawa, N.; Maoka, N.; Masui, R.; Kuramitsu, S.; Kamiya, N.
Structure of P-protein of the glycine cleavage system: implications for nonketotic hyperglycinemia (2005), EMBO J., 24, 1523-1536.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.4.4.2	vapour diffusion method with 30% w/v polyethylene glycol 3350 and 100 mM KSCN as the precipitant. Crystal structure of three forms of P-protein: the apoenzyme at 2.4 A resolution, the holoenzyme at 2.1 A resolution and the holoenzyme in complex with a substrate analog inhibitor (aminooxy)acetate	Thermus thermophilus

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
1.4.4.2	Aminooxyacetate	-	Thermus thermophilus

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.4.4.2	Thermus thermophilus	-	-	-
1.4.4.2	Thermus thermophilus HB8 / ATCC 27634 / DSM 579	-	-	-

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.4.4.2	pyridoxal 5'-phosphate	binding to the apoenzyme induces large open-closed conformational changes, with residues moving up to 13.5 A	Thermus thermophilus

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Release 2023.1 (January 2023)