EC |
2.3.1.264 |
Accepted name: |
β-lysine N6-acetyltransferase |
Reaction: |
acetyl-CoA + (3S)-3,6-diaminohexanoate = CoA + (3S)-6-acetamido-3-aminohexanoate |
Glossary: |
(3S)-3,6-diaminohexanoate = β-L-lysine
(3S)-6-acetamido-3-aminohexanoate = N6-acetyl-β-L-lysine |
Other name(s): |
ablB (gene name) |
Systematic name: |
acetyl-CoA:(3S)-3,6-diaminohexanoate N6-acetyltransferase |
Comments: |
The enzyme is found in some methanogenic archaea and bacteria. In archaea it is induced under salt stress. The product, N6-acetyl-β-L-lysine, serves as a compatible solute, conferring high salt resistance on the producing organisms. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Pfluger, K., Baumann, S., Gottschalk, G., Lin, W., Santos, H. and Muller, V. Lysine-2,3-aminomutase and β-lysine acetyltransferase genes of methanogenic archaea are salt induced and are essential for the biosynthesis of Nε-acetyl-β-lysine and growth at high salinity. Appl. Environ. Microbiol. 69 (2003) 6047–6055. [DOI] [PMID: 14532061] |
2. |
Muller, S., Hoffmann, T., Santos, H., Saum, S.H., Bremer, E. and Muller, V. Bacterial abl-like genes: production of the archaeal osmolyte N(ε)-acetyl-β-lysine by homologous overexpression of the yodP-kamA genes in Bacillus subtilis. Appl. Microbiol. Biotechnol. 91 (2011) 689–697. [DOI] [PMID: 21538109] |
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[EC 2.3.1.264 created 2017] |
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EC |
5.4.3.2 |
Accepted name: |
lysine 2,3-aminomutase |
Reaction: |
L-lysine = (3S)-3,6-diaminohexanoate |
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For diagram of lysine catabolism, click here |
Systematic name: |
L-lysine 2,3-aminomutase |
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. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9075-20-1 |
References: |
1. |
Zappia, V. and Barker, H.A. Studies on lysine-2,3-aminomutase. Subunit structure and sulfhydryl groups. Biochim. Biophys. Acta 207 (1970) 505–513. [DOI] [PMID: 5452674] |
2. |
Aberhart, D.J., Lim, H.-J. and Weiller, B.H. Stereochemistry of lysine 2,3-aminomutase. J. Am. Chem. Soc. 103 (1981) 6750–6752. |
3. |
Frey, P.A. Lysine 2,3-aminomutase: is adenosylmethionine a poor man’s adenosylcobalamin. FASEB J. 7 (1993) 662–670. [PMID: 8500691] |
4. |
Lieder, K.W., Booker, S., Ruzicka, F.J., Beinert, H., Reed, G.H. and Frey, P.A. S-Adenosylmethionine-dependent reduction of lysine 2,3-aminomutase and observation of the catalytically functional iron-sulfur centers by electron paramagnetic resonance. Biochemistry 37 (1998) 2578–2585. [DOI] [PMID: 9485408] |
5. |
Lepore, B.W., Ruzicka, F.J., Frey, P.A. and Ringe, D. The x-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale. Proc. Natl. Acad. Sci. USA 102 (2005) 13819–13824. [DOI] [PMID: 16166264] |
6. |
Frey, P.A. and Reed, G.H. Pyridoxal-5′-phosphate as the catalyst for radical isomerization in reactions of PLP-dependent aminomutases. Biochim. Biophys. Acta 1814 (2011) 1548–1557. [DOI] [PMID: 21435400] |
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[EC 5.4.3.2 created 1972] |
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EC |
5.4.3.3 |
Accepted name: |
lysine 5,6-aminomutase |
Reaction: |
(1) (3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate (2) D-lysine = (2R,5S)-2,5-diaminohexanoate |
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For diagram of lysine catabolism, click here |
Other name(s): |
β-lysine 5,6-aminomutase; β-lysine mutase; L-β-lysine 5,6-aminomutase; D-lysine 5,6-aminomutase; D-α-lysine mutase; adenosylcobalamin-dependent D-lysine 5,6-aminomutase |
Systematic name: |
(3S)-3,6-diaminohexanoate 5,6-aminomutase |
Comments: |
This enzyme is a member of the AdoMet radical (radical SAM) family. It requires pyridoxal 5′-phosphate and adenosylcobalamin for activity. A 5′-deoxyadenosyl radical is generated during the reaction cycle by reductive cleavage of adenosylcobalamin, which is regenerated at the end of the reaction. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9075-69-8 |
References: |
1. |
Stadtman, T.C. and Tasi, L. A cobamide coenzyme dependent migration of the ε-amino group of D-lysine. Biochem. Biophys. Res. Commun. 28 (1967) 920–926. [DOI] [PMID: 4229021] |
2. |
Stadtman, T.C. and Renz, P. Anaerobic degradation of lysine. V. Some properties of the cobamide coenzyme-dependent β-lysine mutase of Clostridium sticklandii. Arch. Biochem. Biophys. 125 (1968) 226–239. [DOI] [PMID: 5649516] |
3. |
Morley, C.G.D. and Stadtman, T.C. Studies on the fermentation of D-α-lysine. Purification and properties of an adenosine triphosphate regulated B12-coenzyme-dependent D-α-lysine mutase complex from Clostridium sticklandii. Biochemistry 9 (1970) 4890–4900. [PMID: 5480154] |
4. |
Retey, J., Kunz, F., Arigoni, D. and Stadtman, T.C. Zur Kenntnis der β-Lysin-Mutase-Reaktion: mechanismus und sterischer Verlauf. Helv. Chim. Acta 61 (1978) 2989–2998. |
5. |
Chang, C.H. and Frey, P.A. Cloning, sequencing, heterologous expression, purification, and characterization of adenosylcobalamin-dependent D-lysine 5, 6-aminomutase from Clostridium sticklandii. J. Biol. Chem. 275 (2000) 106–114. [DOI] [PMID: 10617592] |
6. |
Tang, K.H., Harms, A. and Frey, P.A. Identification of a novel pyridoxal 5′-phosphate binding site in adenosylcobalamin-dependent lysine 5,6-aminomutase from Porphyromonas gingivalis. Biochemistry 41 (2002) 8767–8776. [DOI] [PMID: 12093296] |
7. |
Tang, K.H., Mansoorabadi, S.O., Reed, G.H. and Frey, P.A. Radical triplets and suicide inhibition in reactions of 4-thia-D- and 4-thia-L-lysine with lysine 5,6-aminomutase. Biochemistry 48 (2009) 8151–8160. [DOI] [PMID: 19634897] |
8. |
Berkovitch, F., Behshad, E., Tang, K.H., Enns, E.A., Frey, P.A. and Drennan, C.L. A locking mechanism preventing radical damage in the absence of substrate, as revealed by the x-ray structure of lysine 5,6-aminomutase. Proc. Natl. Acad. Sci. USA 101 (2004) 15870–15875. [DOI] [PMID: 15514022] |
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[EC 5.4.3.3 created 1972 (EC 5.4.3.4 created 1972, incorporated 2017), modified 2017] |
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