Literature summary for 2.3.2.17 extracted from

Schneider, T.; Senn, M.M.; Berger-Bachi, B.; Tossi, A.; Sahl, H.G.; Wiedemann, I.
In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-Gly5) of Staphylococcus aureus (2004), Mol. Microbiol., 53, 675-685.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression as His-tagged protein in Escherichia coli	Staphylococcus aureus

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus aureus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine + 2 glycyl-tRNA	i.e. lipid II-Gly. Enzyme is specific for lipid II-Gly as acceptor	Staphylococcus aureus	N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-triglycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine + 2 tRNA	-	?

Synonyms

Synonyms	Comment	Organism
FemA	-	Staphylococcus aureus

General Information

General Information	Comment	Organism
physiological function	FemA catalyzes the second step in the synthesis of the pentaglycine interpeptide bridge crosslinking different glycan strands in Staphylococcus aureus. FemX adds the first glycine residue to MurNAc-L-Ala-D-Glu-(N6-Gly)L-Lys-D-Ala-D-Ala-diphosphoundecaprenyl-M-acetylglucosamine, i.e. lipid II. Addition of glycine residues 2, 3 and glycine residues 4, 5 is catalyzed by enzymes FemA and FemB, respectively. None of the FemABX enzymes requires the presence of one or two of the other Fem proteins for activity, rather, bridge formation is delayed in an in vitro system when all 3 enzymes are present	Staphylococcus aureus

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Release 2023.1 (January 2023)