The enzyme participates in an L-lysine biosynthetic pathways in certain species of archaea and bacteria. In some organisms the enzyme also catalyses the activity of EC 3.5.1.132, [amino group carrier protein]-ornithine hydrolase.
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
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SYSTEMATIC NAME
IUBMB Comments
[amino group carrier protein]-C-terminal-gamma-L-lysyl-L-glutamate amidohydrolase
The enzyme participates in an L-lysine biosynthetic pathways in certain species of archaea and bacteria. In some organisms the enzyme also catalyses the activity of EC 3.5.1.132, [amino group carrier protein]-ornithine hydrolase.
for the conversion of alpha-aminoadipate to lysine, the amino group of alpha-aminoadipate is modified by attachment to the gamma-carboxyl group of the C-terminal Glu54 of a small protein, LysW. The side chain of alpha-aminoadipate is converted to the lysyl side chain while still attached to LysW, and lysine is subsequently liberated from the LysW-lysine fusion
purified LysK protein has deacetylating activities for both N2-acetyllysine and N2-acetylornithine at almost equal efficiency, reactions of EC 3.5.1.16 and EC 3.5.1.17, respectively
for the conversion of alpha-aminoadipate to lysine, the amino group of alpha-aminoadipate is modified by attachment to the gamma-carboxyl group of the C-terminal Glu54 of a small protein, LysW. The side chain of alpha-aminoadipate is converted to the lysyl side chain while still attached to LysW, and lysine is subsequently liberated from the LysW-lysine fusion
for the conversion of alpha-aminoadipate to lysine, the amino group of alpha-aminoadipate is modified by attachment to the gamma-carboxyl group of the C-terminal Glu54 of a small protein, LysW. The side chain of alpha-aminoadipate is converted to the lysyl side chain while still attached to LysW, and lysine is subsequently liberated from the LysW-lysine fusion
for the conversion of alpha-aminoadipate to lysine, the amino group of alpha-aminoadipate is modified by attachment to the gamma-carboxyl group of the C-terminal Glu54 of a small protein, LysW. The side chain of alpha-aminoadipate is converted to the lysyl side chain while still attached to LysW, and lysine is subsequently liberated from the LysW-lysine fusion
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
LysK in complex with lysine at a resolution of 2.4 A. The alpha-amino group of the bound lysine is oriented toward the catalytic center, which is composed of the residues coordinating divalent metal ions for the hydrolysis of the isopeptide bond. An 11 A long path leads from the active site binding lysine to the protein surface. A positively-charged surface region is located around the exit of the path
Crystal structure of LysK, an enzyme catalyzing the last step of lysine biosynthesis in Thermus thermophilus, in complex with lysine Insight into the mechanism for recognition of the amino-group carrier protein, LysW