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Information on EC 3.5.1.130 - [amino group carrier protein]-lysine hydrolase and Organism(s) Thermus thermophilus and UniProt Accession Q8VUS5

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IUBMB Comments
The enzyme participates in an L-lysine biosynthetic pathway 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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This record set is specific for:
Thermus thermophilus
UNIPROT: Q8VUS5
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The taxonomic range for the selected organisms is: Thermus thermophilus
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Reaction Schemes
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[amino group carrier protein]-C-terminal-gamma-(L-lysyl)-L-glutamate
+
H2O
=
[amino group carrier protein]-C-terminal-L-glutamate
+
L-lysine
[amino group carrier protein]-C-terminal-gamma-(L-lysyl)-L-glutamate
+
=
[amino group carrier protein]-C-terminal-L-glutamate
+
Synonyms
lysK, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lysK
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PATHWAY SOURCE
PATHWAYS
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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 pathway 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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[carrier protein LysW]-C-terminal-gamma-(L-lysyl)-L-glutamate + H2O
[carrier protein LysW]-C-terminal-L-glutamate + L-lysine
show the reaction diagram
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-
-
?
[CT10-LysW]-C-terminal-gamma-(L-lysyl)-L-glutamate + H2O
[CT10-LysW]-C-terminal-L-glutamate + L-lysine
show the reaction diagram
i.e. the C-terminal 10 residues of LysW fused with one lysine residue at its gamma-carboxyl group of C-terminal Glu54
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-
?
additional information
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
[carrier protein LysW]-C-terminal-gamma-(L-lysyl)-L-glutamate + H2O
[carrier protein LysW]-C-terminal-L-glutamate + L-lysine
show the reaction diagram
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-
-
?
additional information
?
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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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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
[carrier protein LysW]-C-terminal-alpha-(L-lysyl)-L-glutamate
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
36 - 530
[carrier protein LysW]-C-terminal-gamma-(L-lysyl)-L-glutamate
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3.1 - 5.5
[CT10-LysW]-C-terminal-gamma-(L-lysyl)-L-glutamate
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00067
[carrier protein LysW]-C-terminal-alpha-(L-lysyl)-L-glutamate
Thermus thermophilus
pH 8.0, 60°C
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
a knockout mutant shows significantly slow growth on a minimal medium, and the growth is markedly improved by addition of lysine
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D325A
marked decrease in activity
K297E
marked decrease in activity
R282E
marked decrease in activity
R286E
marked decrease in activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fujita, S.; Cho, S.H.; Yoshida, A.; Hasebe, F.; Tomita, T.; Kuzuyama, T.; Nishiyama, M.
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
Biochem. Biophys. Res. Commun.
491
409-415
2017
Thermus thermophilus (Q8VUS5)
Manually annotated by BRENDA team
Miyazaki, J.; Kobashi, N.; Fujii, T.; Nishiyama, M.; Yamane, H.
Characterization of a lysK gene as an argE homolog in Thermus thermophilus HB27
FEBS Lett.
512
269-274
2002
Thermus thermophilus (Q8VUS5)
Manually annotated by BRENDA team
Horie, A.; Tomita, T.; Saiki, A.; Kono, H.; Taka, H.; Mineki, R.; Fujimura, T.; Nishiyama, C.; Kuzuyama, T.; Nishiyama, M.
Discovery of proteinaceous N-modification in lysine biosynthesis of Thermus thermophilus
Nat. Chem. Biol.
5
673-679
2009
Thermus thermophilus (Q8VUS5), Thermus thermophilus DSM 7039 (Q8VUS5)
Manually annotated by BRENDA team