Weak gamma-glutamyl:cysteine ligase; ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity. However, because of the low catalytic rate, the question remains whether L-cysteine is the actual biological substrate; Belongs to the glutamate--cysteine ligase type 2 family. YbdK subfamily.

fructose-1-P and 6-phosphogluconate phosphatase; Catalyzes strongly the dephosphorylation of fructose-1- phosphate (Fru1P) and slightly the dephosphorylation of 6- phosphogluconate (6P-Glu). It has low beta-phosphoglucomutase activity.

Cytosol non-specific dipeptidase; Dipeptidase with broad substrate specificity. Requires dipeptide substrates with an unblocked N-terminus and the amino group in the alpha or beta position. Non-protein amino acids and proline are not accepted in the C-terminal position, whereas some dipeptide amides and formyl amino acids are hydrolyzed. Also shows cysteinylglycinase activity, which is sufficient for E.coli to utilize cysteinylglycine as a cysteine source.

Aminopeptidase N; Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation.

Gamma-glutamyltranspeptidase; Cleaves the gamma-glutamyl bond of periplasmic glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases; it may function in amino acid uptake/salvage, or possibly in peptidoglycan linkage. Catalyzes the hydrolysis and transpeptidation of many gamma-glutamyl compounds (including some D- gamma-glutamyl substrates), with a preference for basic and aromatic amino acids as acce [...]

Aminopeptidase B; Probably plays an important role in intracellular peptide degradation.

Cytosol aminopeptidase; Probably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Required for plasmid ColE1 site-specific recombination but not in its aminopeptidase activity. Could act as a structural component of the putative nucleoprotein complex in which the Xer recombination reaction takes place.

Putative allophanate hydrolase, subunit 1; Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate. Belongs to the PxpB family.

Putative allophanate hydrolase, subunit 2; Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate. Belongs to the PxpC family.