Literature summary for 1.4.1.27 extracted from

Fujiwara, K.; Okamura-Ikeda, K.; Motokawa, Y.
Expression of mature bovine H-protein of the glycine cleavage system in Escherichia coli and in vitro lipoylation of the apoform (1992), J. Biol. Chem., 267, 20011-20016 .

Search for more literature for 1.4.1.27

Application

Application	Comment	Organism
synthesis	recombinant expression of H-protein in Escherichia coli. When the cells are cultured in medium supplemented with 30 microM lipoate, about 10% of the protein expressed is the correctly lipoylated active form, 10% is an inactive aberrantly modified form, and the remaining 80% is the unlipoylated apoform	Bos taurus

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli, soluble protein	Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	P20821	P20821 i.e. H-protein, lipoyl-carrier protein	-

Purification (Commentary)

Purification (Comment)	Organism
the purified recombinant apo-H-protein is lipoylated and consequently activated in vitro with lipoyl-AMP as a lipoyl donor by lipoyltransferase	Bos taurus

Subunits

Subunits	Comment	Organism
?	x * 14000, SDS-PAGE, recombinant H-protein	Bos taurus

Synonyms

Synonyms	Comment	Organism
GCSH	-	Bos taurus

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Release 2023.1 (January 2023)