KEGG   ENZYME: 5.4.3.3Help
Entry
EC 5.4.3.3                  Enzyme                                 

Name
lysine 5,6-aminomutase;
beta-lysine 5,6-aminomutase;
beta-lysine mutase;
L-beta-lysine 5,6-aminomutase;
D-lysine 5,6-aminomutase;
D-alpha-lysine mutase;
adenosylcobalamin-dependent D-lysine 5,6-aminomutase
Class
Isomerases;
Intramolecular transferases;
Transferring amino groups
BRITE hierarchy
Sysname
(3S)-3,6-diaminohexanoate 5,6-aminomutase
Reaction(IUBMB)
(1) (3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate [RN:R03275];
(2) D-lysine = (2R,5S)-2,5-diaminohexanoate [RN:R02852]
Reaction(KEGG)
Substrate
(3S)-3,6-diaminohexanoate [CPD:C01142];
D-lysine [CPD:C00739]
Product
(3S,5S)-3,5-diaminohexanoate [CPD:C01186];
(2R,5S)-2,5-diaminohexanoate [CPD:C05161]
Comment
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.
History
EC 5.4.3.3 created 1972 (EC 5.4.3.4 created 1972, incorporated 2017), modified 2017
Pathway
Lysine degradation
Orthology
K01844  
beta-lysine 5,6-aminomutase alpha subunit
K18011  
beta-lysine 5,6-aminomutase beta subunit
Genes
RFR: 
AZA: 
AZI: 
ADE: 
ACP: 
AFW: 
ANK: 
MXA: 
MXAN_4386(kamE) MXAN_4388(kamD)
MFU: 
MSD: 
MYM: 
CCX: 
SUR: 
AGE: 
VIN: 
SCL: 
sce2889(kamD) sce2891(kamE)
SCU: 
CCRO: 
LLU: 
MRM: 
TUM: 
CLS: 
CPAT: 
CPAE: 
CEU: 
AMT: 
AOE: 
GFE: 
CST: 
STH: 
DAI: 
IBU: 
FPLA: 
EUU: 
TTE: 
TWI: 
NTH: 
HPK: 
PUF: 
PFT: 
MBJ: 
SCX: 
ICA: 
ARS: 
NCA: 
KFL: 
TCU: 
MMAR: 
SESP: 
KAL: 
KPHY: 
LED: 
ALL: 
STP: 
SAQ: 
MAU: 
MIL: 
VMA: 
AMS: 
ASE: 
ACTN: 
AFS: 
SNA: 
FNU: 
FNC: 
FNT: 
FUS: 
FNE: 
FHW: 
BACC: 
PGI: 
PG_1073(kamD) PG_1074(kamE)
PGN: 
PGT: 
PAH: 
OSP: 
CACI: 
CLOAM1503(kamE) CLOAM1504(kamD)
TLE: 
PHY: 
TME: 
TAF: 
THP: 
THER: 
FNO: 
FPE: 
FIA: 
PMO: 
MPZ: 
MARN: 
KOL: 
KPF: 
MPG: 
 » show all
Taxonomy
Reference
1  [PMID:4229021]
  Authors
Stadtman TC, Tsai L.
  Title
A cobamide coenzyme dependent migration of the epsilon-amino group of D-lysine.
  Journal
Biochem. Biophys. Res. Commun. 28 (1967) 920-6.
Reference
2  [PMID:5649516]
  Authors
Stadtman TC, Renz P.
  Title
Anaerobic degradation of lysine. V. Some properties of the cobamide coenzyme-dependent beta-lysine mutase of Clostridium sticklandii.
  Journal
Arch. Biochem. Biophys. 125 (1968) 226-39.
Reference
3  [PMID:5480154]
  Authors
Morley CG, Stadtman TC.
  Title
Studies on the fermentation of D-alpha-lysine. Purification and properties of an adenosine triphosphate regulated B 12-coenzyme-dependent D-alpha-lysine mutase complex from Clostridium sticklandii.
  Journal
Biochemistry. 9 (1970) 4890-900.
Reference
4
  Authors
Retey, J., Kunz, F., Arigoni, D. and Stadtman, T.C.
  Title
Zur Kenntnis der beta-Lysin-Mutase-Reaktion: mechanismus und sterischer Verlauf.
  Journal
Helv. Chim. Acta 61 (1978) 2989-2998.
Reference
5  [PMID:10617592]
  Authors
Chang CH, Frey PA
  Title
Cloning, sequencing, heterologous expression, purification, and characterization  of adenosylcobalamin-dependent D-lysine 5, 6-aminomutase from Clostridium sticklandii.
  Journal
J. Biol. Chem. 275 (2000) 106-14.
  Sequence
Reference
6  [PMID:12093296]
  Authors
Tang KH, Harms A, Frey PA
  Title
Identification of a novel pyridoxal 5'-phosphate binding site in adenosylcobalamin-dependent lysine 5,6-aminomutase from Porphyromonas gingivalis.
  Journal
Biochemistry. 41 (2002) 8767-76.
Reference
7  [PMID:19634897]
  Authors
Tang KH, Mansoorabadi SO, Reed GH, Frey PA
  Title
Radical triplets and suicide inhibition in reactions of 4-thia-D- and 4-thia-L-lysine with lysine 5,6-aminomutase.
  Journal
Biochemistry. 48 (2009) 8151-60.
Reference
8  [PMID:15514022]
  Authors
Berkovitch F, Behshad E, Tang KH, Enns EA, Frey PA, Drennan CL
  Title
A locking mechanism preventing radical damage in the absence of substrate, as revealed by the x-ray structure of lysine 5,6-aminomutase.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 15870-5.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9075-69-8

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