Reference on EC 5.4.3.2 - lysine 2,3-aminomutase
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chirpich, T.P.; Zappia, V.; Costilow, R.N.; Barker, H.A.
Lysine 2,3-aminomutase. Purification and properties of a pyridoxal phosphate and S-adenosylmethionine-activated enzyme
J. Biol. Chem.
245
1778-1789
1970
Clostridium sp., Clostridium sp. SB4
Zappia, V.; Barker, H.A.
Studies on lysine-2,3-aminomutase. Subunit structure and sulfhydryl groups
Biochim. Biophys. Acta
207
505-513
1970
Clostridium sp., Clostridium sp. SB4
Chirpich, T.P.; Barker, H.A.
Lysine-2,3-aminomutase (Clostridium)
Methods Enzymol.
17B
215-222
1971
Clostridium sp., Clostridium sp. SB4
-
Barker, H.A.; Kahn, J.M.; Hedrick, L.
Pathway of lysine degradation in Fusobacterium nucleatum
J. Bacteriol.
152
201-207
1982
Fusobacterium nucleatum
Aberhart, D.J.; Gould, S.J.; Lin, H.J.; Thiruvengadam, T.K.; Weiller, B.H.
Stereochemistry of lysine 2,3-aminomutase isolated from Clostridium subterminale strain SB4
J. Am. Chem. Soc.
105
5461-5470
1983
Clostridium subterminale, Clostridium subterminale SB4
-
Thiruvengadam, T.K.; Gould, S.J.; Aberhart, D.J.; Lin, H.J.
Biosynthesis of Streptothricin F. 5. Formation of beta-lysine by Streptomyces L-1689-23
J. Am. Chem. Soc.
105
5470-5476
1983
Streptomyces sp., Streptomyces sp. L-1689-23
-
Petrovich, R.M.; Ruzicka, F.J.; Reed, G.H.; Frey, P.A.
Metal cofactors of lysine-2,3-aminomutase
J. Biol. Chem.
266
7656-7660
1991
Clostridium sp., Clostridium sp. SB4
Song, K.B.; Frey, P.A.
Molecular properties of lysine-2,3-aminomutase
J. Biol. Chem.
266
7651-7655
1991
Clostridium subterminale, Clostridium subterminale SB4
Aberhart, D.J.
Studies of the mechanism of lysine 2,3-aminomutase
J. Chem. Soc. Perkin Trans. I
1988
343-350
1988
Clostridium subterminale, Clostridium subterminale SB4
-
Aberhart, D.J.; Cotting, J.A.
Mechanistic studies on lysine 2,3-aminomutase: carbon-13-deuterium crossover experiments
J. Chem. Soc. Perkin Trans. I
1988
2119-2122
1988
Clostridium subterminale
-
Frey, P.A.; Reed, G.H.
Lysine 2,3-aminomutase and the mechanism of the interconversion of lysine and beta-lysine
Adv. Enzymol. Relat. Areas Mol. Biol.
66
1-39
1993
Clostridium sp.
Frey, P.A.; Moss, M.; Petrovich, R.; Baraniak, J.
The roles of S-adenosylmethionine and pyridoxal phosphate in the lysine 2,3-aminomutase reaction
Ann. N. Y. Acad. Sci.
585
368-378
1990
Clostridium sp.
Frey, P.A.; Ballinger, M.D.; Reed, G.H.
S-Adenosylmethionine: a "poor man's coenzyme B12" in the reaction of lysine 2,3-aminomutase
Biochem. Soc. Trans.
26
304-310
1998
Clostridium sp.
Lieder, K.W.; Booker, S.; Ruzicka, F.J.; Beinert, H.; Reed, G.H.; 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
2578-2585
1998
Clostridium subterminale
Frey, P.A.
Lysine 2,3-aminomutase: is adenosylmethionine a poor man's adenosylcobalamin?
FASEB J.
7
662-670
1993
Clostridium subterminale
Moss, M.L.; Frey, P.A.
Activation of lysine 2,3-aminomutase by S-adenosylmethionine
J. Biol. Chem.
265
18112-18115
1990
Clostridium sp., Clostridium sp. SB4
Baraniak, J.; Moss, M.L.; Frey, P.A.
Lysine 2,3-aminomutase. Support for a mechanism of hydrogen transfer involving S-adenosylmethionine
J. Biol. Chem.
264
1357-1360
1989
Clostridium sp., Clostridium sp. SB4
Ballinger, M.D.; Frey, P.A.; Reed, G.H.; LoBrutto, R.
Pulsed electron paramagnetic resonance studies of the lysine 2,3-aminomutase substrate radical: evidence for participation of pyridoxal 5'-phosphate in a radical rearrangement
Biochemistry
34
10086-10093
1995
Clostridium sp., Clostridium sp. SB4
Ballinger, M.D.; Frey, P.A.; Reed, G.H.
Structure of a substrate radical intermediate in the reaction of lysine 2,3-aminomutase
Biochemistry
31
10782-10789
1992
Clostridium sp.
Ballinger, M.D.; Reed, G.H.; Frey, P.A.
An organic radical in the lysine 2,3-aminomutase reaction
Biochemistry
31
949-953
1992
Clostridium sp.
Chen, D.; Ruzicka, F.J.; Frey, P.A.
A novel lysine 2,3-aminomutase encoded by the yodO gene of Bacillus subtilis: characterization and the observation of organic radical intermediates
Biochem. J.
348
539-549
2000
Bacillus subtilis
Cosper, N.J.; Booker, S.J.; Ruzicka, F.; Frey, P.A.; Scott, R.A.
Direct FeS cluster involvement in generation of a radical in lysine 2,3-aminomutase
Biochemistry
39
15668-15673
2000
Clostridium subterminale
Wu, W.; Booker, S.; Lieder, K.W.; Bandarian, V.; Reed, G.H.; Frey, P.A.
Lysine 2,3-aminomutase and trans-4,5-dehydrolysine: characterization of an allylic analogue of a substrate-based radical in the catalytic mechanism
Biochemistry
39
9561-9570
2000
Clostridium subterminale
Chen, D.; Walsby, C.; Hoffman, B.M.; Frey, P.A.
Coordination and mechanism of reversible cleavage of S-adenosylmethionine by the [4Fe-4S] center in lysine 2,3-aminomutase
J. Am. Chem. Soc.
125
11788-11789
2003
Clostridium subterminale
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, Methanosarcina mazei (Q8PYC9), Methanosarcina mazei, Methanosarcina mazei DSM 3647 (Q8PYC9), Methanococcus maripaludis DSM 2067 (Q6LYX4)
Lepore, B.W.; Ruzicka, F.J.; Frey, P.A.; Ringe, D.
The X-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale
Proc. Natl. Acad. Sci. USA
102
13819-13824
2005
Clostridium subterminale (Q9XBQ8), Clostridium subterminale
Brazeau, B.J.; Gort, S.J.; Jessen, H.J.; Andrew, A.J.; Liao, H.H.
Enzymatic activation of lysine 2,3-aminomutase from Porphyromonas gingivalis
Appl. Environ. Microbiol.
72
6402-6404
2006
Porphyromonas gingivalis
Behshad, E.; Ruzicka, F.J.; Mansoorabadi, S.O.; Chen, D.; Reed, G.H.; Frey, P.A.
Enantiomeric free radicals and enzymatic control of stereochemistry in a radical mechanism: the case of lysine 2,3-aminomutases
Biochemistry
45
12639-12646
2006
Clostridium subterminale, Escherichia coli
Chen, D.; Frey, P.A.; Lepore, B.W.; Ringe, D.; Ruzicka, F.J.
Identification of structural and catalytic classes of highly conserved amino acid residues in lysine 2,3-aminomutase
Biochemistry
45
12647-12653
2006
Clostridium subterminale (Q9XBQ8), Clostridium subterminale SB4 (Q9XBQ8), Clostridium subterminale SB4
Hinckley, G.T.; Frey, P.A.
Cofactor dependence of reduction potentials for [4Fe-4S]2+/1+ in lysine 2,3-aminomutase
Biochemistry
45
3219-3225
2006
Clostridium subterminale, Clostridium subterminale SB4
Wang, S.C.; Frey, P.A.
Binding energy in the one-electron reductive cleavage of S-adenosylmethionine in lysine 2,3-aminomutase, a radical SAM enzyme
Biochemistry
46
12889-12895
2007
Clostridium subterminale, Clostridium subterminale SB4
Chen, D.; Tanem, J.; Frey, P.A.
Basis for the equilibrium constant in the interconversion of L-lysine and L-beta-lysine by lysine 2,3-aminomutase
Biochim. Biophys. Acta
1774
297-302
2007
Clostridium subterminale, Clostridium subterminale SB4
Lees, N.S.; Chen, D.; Walsby, C.J.; Behshad, E.; Frey, P.A.; Hoffman, B.M.
How an enzyme tames reactive intermediates: positioning of the active-site components of lysine 2,3-aminomutase during enzymatic turnover as determined by ENDOR spectroscopy
J. Am. Chem. Soc.
128
10145-10154
2006
Clostridium subterminale, Clostridium subterminale SB4
Frey, P.A.; Hegeman, A.D.; Ruzicka, F.J.
The radical SAM superfamily
Crit. Rev. Biochem. Mol. Biol.
43
63-88
2008
Clostridium subterminale (Q9XBQ8)
Saum, R.; Mingote, A.; Santos, H.; Mueller, V.
A novel limb in the osmoregulatory network of Methanosarcina mazei Goe1: N(epsilon)-acetyl-beta-lysine can be substituted by glutamate and alanine
Environ. Microbiol.
11
1056-1065
2009
Methanosarcina mazei Go1
Frey, P.A.; Reed, G.H.
Pyridoxal-5'-phosphate as the catalyst for radical isomerization in reactions of PLP-dependent aminomutases
Biochim. Biophys. Acta
1814
1548-1557
2011
Clostridium subterminale, Clostridium subterminale SB4
Ruzicka, F.J.; Frey, P.A.
Kinetic and spectroscopic evidence of negative cooperativity in the action of lysine 2,3-aminomutase
J. Phys. Chem. B
114
16118-16124
2010
Clostridium subterminale, Clostridium subterminale SB4
Park, J.H.; Johansson, H.E.; Aoki, H.; Huang, B.X.; Kim, H.Y.; Ganoza, M.C.; Park, M.H.
Post-translational modification by beta-lysylation is required for activity of Escherichia coli elongation factor P (EF-P)
J. Biol. Chem.
287
2579-2590
2012
Escherichia coli, Escherichia coli K-16
Hung, C.C.; Lai, M.C.
The phylogenetic analysis and putative function of lysine 2,3-aminomutase from methanoarchaea infers the potential biocatalysts for the synthesis of beta-lysine
J. Microbiol. Immunol. Infect.
46
1-10
2013
Methanocalculus chunghsingensis (G3F9W8), Methanocalculus chunghsingensis, Methanohalophilus portucalensis (G3F9X2), Methanohalophilus portucalensis, Methanosarcina mazei (Q8PYC9), Methanosarcina mazei DSM 3647 (Q8PYC9), Methanohalophilus portucalensis FDF1 (G3F9X2), Methanocalculus chunghsingensis K1F9705b (G3F9W8)
Stich, T.A.; Myers, W.K.; Britt, R.D.
Paramagnetic intermediates generated by radical S-adenosylmethionine (SAM) enzymes
Acc. Chem. Res.
47
2235-2243
2014
Escherichia coli
Frey, P.
Travels with carbon-centered radicals. 5'-Deoxyadenosine and 5'-deoxyadenosine-5'-yl in radical enzymology
Acc. Chem. Res.
47
540-549
2014
Clostridium subterminale (Q9XBQ8), Clostridium subterminale SB4 (Q9XBQ8)
Horitani, M.; Byer, A.S.; Shisler, K.A.; Chandra, T.; Broderick, J.B.; Hoffman, B.M.
Why nature uses radical SAM enzymes so widely electron nuclear double resonance studies of lysine 2,3-aminomutase show the 5-dAdo? Free radical is never free
J. Am. Chem. Soc.
137
7111-7121
2015
Clostridium subterminale (Q9XBQ8), Clostridium subterminale SB4 (Q9XBQ8), Clostridium subterminale SB4
Zhang, Z.; Yang, M.; Peng, Q.; Wang, G.; Zheng, Q.; Zhang, J.; Song, F.
Transcription of the lysine-2,3-aminomutase gene in the kam locus of Bacillus thuringiensis subsp. kurstaki HD73 is controlled by both sigma54 and sigmaK factors
J. Bacteriol.
196
2934-2943
2014
Bacillus thuringiensis serovar kurstaki (A0A0K0QCW0), Bacillus thuringiensis serovar kurstaki, Bacillus thuringiensis serovar kurstaki HD73 (A0A0K0QCW0)
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