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Literature summary for 1.4.1.27 extracted from

  • Zhang, H.; Li, Y.; Nie, J.; Ren, J.; Zeng, A.P.
    Structure-based dynamic analysis of the glycine cleavage system suggests key residues for control of a key reaction step (2020), Commun. Biol., 3, 756 .
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
S67F mutation in H-protein, significant decrease in activity Escherichia coli
S67P mutation in H-protein, increase in activity Escherichia coli
S67Q mutation in H-protein, significant decrease in activity Escherichia coli
S67T mutation in H-protein, increase in activity Escherichia coli
S67V mutation in H-protein, increase in activity Escherichia coli
S67Y mutation in H-protein, significant decrease in activity Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6T9 component H-protein
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General Information

General Information Comment Organism
physiological function structure-based dynamic analysis of the induced release of the lipoate arm of protein H. Four major steps of the release process can be distinguished showing significantly different energy barriers and time scales. Mutations of key residue, Ser67 in protein H, leads to a bidirectional tuning of the release process Escherichia coli