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Information on EC 3.5.1.130 - [amino group carrier protein]-lysine hydrolase

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EC Tree

3 Hydrolases

3.5 Acting on carbon-nitrogen bonds, other than peptide bonds

3.5.1 In linear amides

3.5.1.130 [amino group carrier protein]-lysine hydrolase

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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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,

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SYNONYM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

lysK

lysK

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REACTION

REACTION DIAGRAM

COMMENTARY

ORGANISM

UNIPROT

LITERATURE

[amino group carrier protein]-C-terminal-gamma-(L-lysyl)-L-glutamate + H2O = [amino group carrier protein]-C-terminal-L-glutamate + L-lysine

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Go to Pathway Search

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PATHWAY SOURCE

PATHWAYS

BRENDA

lysine metabolism

KEGG

Lysine biosynthesis

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SYSTEMATIC NAME

IUBMB Comments

[amino group carrier protein]-C-terminal-gamma-L-lysyl-L-glutamate amidohydrolase

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SUBSTRATE

PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

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

2 entries

[CT10-LysW]-C-terminal-gamma-(L-lysyl)-L-glutamate + H2O

[CT10-LysW]-C-terminal-L-glutamate + L-lysine

Thermus thermophilus

Q8VUS5

i.e. the C-terminal 10 residues of LysW fused with one lysine residue at its gamma-carboxyl group of C-terminal Glu54

749817

additional information

5 entries

[carrier protein LysW]-C-terminal-gamma-(L-lysyl)-L-glutamate + H2O

[carrier protein LysW]-C-terminal-L-glutamate + L-lysine

Thermus thermophilus

Q8VUS5

749817, 751648

[carrier protein LysW]-C-terminal-gamma-(L-lysyl)-L-glutamate + H2O

[carrier protein LysW]-C-terminal-L-glutamate + L-lysine

Thermus thermophilus DSM 7039

Q8VUS5

751648

additional information

Thermus thermophilus

Q8VUS5

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

751648

additional information

Thermus thermophilus

Q8VUS5

no substrates: [carrier protein LysW]-C-terminal-alpha-(L-lysyl)-L-glutamate, [carrier protein LysW]-13-alpha-(L-lysyl)-L-glutamate

751648

additional information

Thermus thermophilus

Q8VUS5

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

750535

additional information

Thermus thermophilus DSM 7039

Q8VUS5

751648

additional information

Thermus thermophilus DSM 7039

Q8VUS5

no substrates: [carrier protein LysW]-C-terminal-alpha-(L-lysyl)-L-glutamate, [carrier protein LysW]-13-alpha-(L-lysyl)-L-glutamate

751648

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

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

2 entries

additional information

2 entries

[carrier protein LysW]-C-terminal-gamma-(L-lysyl)-L-glutamate + H2O

[carrier protein LysW]-C-terminal-L-glutamate + L-lysine

Thermus thermophilus

Q8VUS5

751648

[carrier protein LysW]-C-terminal-gamma-(L-lysyl)-L-glutamate + H2O

[carrier protein LysW]-C-terminal-L-glutamate + L-lysine

Thermus thermophilus DSM 7039

Q8VUS5

751648

additional information

Thermus thermophilus

Q8VUS5

751648

additional information

Thermus thermophilus DSM 7039

Q8VUS5

751648

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

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

LITERATURE

IMAGE

36 - 530

[carrier protein LysW]-C-terminal-gamma-(L-lysyl)-L-glutamate

3 entries

3.1 - 5.5

[CT10-LysW]-C-terminal-gamma-(L-lysyl)-L-glutamate

3 entries

[carrier protein LysW]-C-terminal-gamma-(L-lysyl)-L-glutamate

Thermus thermophilus

Q8VUS5

mutant R286E, pH 8.0, 60°C

749817

[carrier protein LysW]-C-terminal-gamma-(L-lysyl)-L-glutamate

Thermus thermophilus

Q8VUS5

mutant R282E, pH 8.0, 60°C

749817

530

[carrier protein LysW]-C-terminal-gamma-(L-lysyl)-L-glutamate

Thermus thermophilus

Q8VUS5

wild-type, pH 8.0, 60°C

749817

3.1

[CT10-LysW]-C-terminal-gamma-(L-lysyl)-L-glutamate

Thermus thermophilus

Q8VUS5

mutant R286E, pH 8.0, 60°C

749817

4.5

[CT10-LysW]-C-terminal-gamma-(L-lysyl)-L-glutamate

Thermus thermophilus

Q8VUS5

mutant R282E, pH 8.0, 60°C

749817

5.5

[CT10-LysW]-C-terminal-gamma-(L-lysyl)-L-glutamate

Thermus thermophilus

Q8VUS5

wild-type, pH 8.0, 60°C

749817

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IC50 VALUE [mM]

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.00067

[carrier protein LysW]-C-terminal-alpha-(L-lysyl)-L-glutamate

Thermus thermophilus

Q8VUS5

pH 8.0, 60°C

751648

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

Thermus thermophilus

749817, 750535, 751648

Q8VUS5

UniProt

brenda

Thermus thermophilus DSM 7039

751648

Q8VUS5

UniProt

brenda

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

physiological function

Thermus thermophilus

Q8VUS5

a knockout mutant shows significantly slow growth on a minimal medium, and the growth is markedly improved by addition of lysine

750535

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Show AA Sequence and Transmembrane Helices (1275 entries)
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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

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

D325A

Thermus thermophilus

Q8VUS5

marked decrease in activity

749817

K297E

Thermus thermophilus

Q8VUS5

marked decrease in activity

749817

R282E

Thermus thermophilus

Q8VUS5

marked decrease in activity

749817

R286E

Thermus thermophilus

Q8VUS5

marked decrease in activity

749817

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

recombinant protein

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

Thermus thermophilus

Q8VUS5

749817

expression in Escherichia coli

Thermus thermophilus

Q8VUS5

751648

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

749817

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)

28720495

brenda

750535

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)

11852094

brenda

751648

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.

673-679

2009

Thermus thermophilus (Q8VUS5), Thermus thermophilus DSM 7039 (Q8VUS5)

19620981

brenda

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EXTERNAL LINKS (specific for EC-Number 3.5.1.130)

ExplorEnz (official portal for IUBMB Enzyme Nomenclature)

Expasy Enzyme Nomenclature Database

KEGG

MetaCyc

SABIO-RK

NCBI: PubMed, Protein, Nucleotide, Structure, Gene, OMIM

Enzyme Nomenclature (alternative site)

UniProt

PDB

PROSITE Database of protein families and domains

InterPro (database of protein families, domains and functional sites)

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