Enzyme

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     5. Isomerases
        5.4 Intramolecular transferases
            5.4.3 Transferring amino groups
ID:5.4.3.2
Description:Lysine 2,3-aminomutase.
Cath: 1.10.287.2750; 3.20.20.70; 2.40.50.60; 2.40.50.600;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 5.4.3.2
BRENDA Enzyme Link: BRENDA 5.4.3.2
KEGG Enzyme Link: KEGG5.4.3.2
BioCyc Enzyme Link: BioCyc 5.4.3.2
ExPASy Enzyme Link: ExPASy5.4.3.2
EC2PDB Enzyme Link: EC2PDB 5.4.3.2
ExplorEnz Enzyme Link: ExplorEnz 5.4.3.2
PRIAM enzyme-specific profiles Link: PRIAM 5.4.3.2
IntEnz Enzyme Link: IntEnz 5.4.3.2
MEDLINE Enzyme Link: MEDLINE 5.4.3.2
MSA:

5.4.3.2;

Phylogenetic Tree:

5.4.3.2;

Uniprot:
M-CSA:
RHEA:19177 L-lysine = (3S)-3,6-diaminohexanoate
RULE(radius=1) [*:1]-[CH;+0:2](-[NH2;+0:3])-[CH2;+0:4]-[*:5]>>[*:1]-[CH2;+0:2]-[CH;+0:4](-[*:5])-[NH2;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
S-adenosylmethionine: a 'poor man's coenzyme B12' in the reaction of lysine 2,3-aminomutase.Frey PA, Ballinger MD, Reed GH1998 Aug9765869
S-Adenosylmethionine-dependent reduction of lysine 2,3-aminomutase and observation of the catalytically functional iron-sulfur centers by electron paramagnetic resonance.Lieder KW, Booker S, Ruzicka FJ, Beinert H, Reed GH, Frey PA1998 Feb 249485408
Lysine 2,3-aminomutase and the mechanism of the interconversion of lysine and beta-lysine.Frey PA, Reed GH19938430513
Lysine 2,3-aminomutase. Purification and properties of a pyridoxal phosphate and S-adenosylmethionine-activated enzyme.Chirpich TP, Zappia V, Costilow RN, Barker HA1970 Apr 105438361
Lysine 2,3-aminomutase from Clostridium subterminale SB4: mass spectral characterization of cyanogen bromide-treated peptides and cloning, sequencing, and expression of the gene kamA in Escherichia coli.Ruzicka FJ, Lieder KW, Frey PA2000 Jan10629195
Pathway of lysine degradation in Fusobacterium nucleatum.Barker HA, Kahn JM, Hedrick L1982 Oct6811551