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Information on EC 5.4.3.2 - lysine 2,3-aminomutase and Organism(s) Methanococcus maripaludis and UniProt Accession Q6LYX4

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EC Tree
     5 Isomerases
         5.4 Intramolecular transferases
             5.4.3 Transferring amino groups
                5.4.3.2 lysine 2,3-aminomutase
IUBMB Comments
This enzyme is a member of the 'AdoMet radical' (radical SAM) family. It contains pyridoxal phosphate and a [4Fe-4S] cluster and binds an exchangeable S-adenosyl-L-methionine molecule. Activity in vitro requires a strong reductant such as dithionite and strictly anaerobic conditions. A 5'-deoxyadenosyl radical is generated during the reaction cycle by reductive cleavage of S-adenosyl-L-methionine, mediated by the iron-sulfur cluster. S-adenosyl-L-methionine is regenerated at the end of the reaction.
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Methanococcus maripaludis
UNIPROT: Q6LYX4
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Word Map
The taxonomic range for the selected organisms is: Methanococcus maripaludis
The enzyme appears in selected viruses and cellular organisms
Synonyms
lysine 2,3-aminomutase, lysine-2,3-aminomutase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Aminomutase, lysine 2,3-
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L-Lysine-2,3-aminomutase
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Mutase, lysine 2,3-amino-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
L-lysine 2,3-aminomutase
This enzyme is a member of the 'AdoMet radical' (radical SAM) family. It contains pyridoxal phosphate and a [4Fe-4S] cluster and binds an exchangeable S-adenosyl-L-methionine molecule. Activity in vitro requires a strong reductant such as dithionite and strictly anaerobic conditions. A 5'-deoxyadenosyl radical is generated during the reaction cycle by reductive cleavage of S-adenosyl-L-methionine, mediated by the iron-sulfur cluster. S-adenosyl-L-methionine is regenerated at the end of the reaction.
CAS REGISTRY NUMBER
COMMENTARY hide
9075-20-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
DELTAabl mutants of Methanococcus maripaludis no longer produced Nepsilon-acetyl-beta-lysine and are incapable of growth at high salt concentrations, indicating that the abl operon is essential for Nepsilon-acetyl-beta-lysine synthesis
physiological function
the enzyme is involved in the biosynthesis of Nepsilon-acetyl-beta-lysine, that is accumulated in the cells to respond to an osmotic upshock
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of the abl operon is strictly salt dependent
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pfluger, K.; Baumann, S.; Gottschalk, G.; Lin, W.; Santos, H.; Muller, V.
Lysine-2,3-aminomutase and beta-lysine acetyltransferase genes of methanogenic archaea are salt induced and are essential for the biosynthesis of Nepsilon-acetyl-beta-lysine and growth at high salinity
Appl. Environ. Microbiol.
69
6047-6055
2003
Methanococcus maripaludis (Q6LYX4), Methanococcus maripaludis, Methanococcus maripaludis DSM 2067 (Q6LYX4), Methanosarcina mazei (Q8PYC9), Methanosarcina mazei, Methanosarcina mazei DSM 3647 (Q8PYC9)
Manually annotated by BRENDA team