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
ec00310  Lysine degradation
Orthology
K01844  beta-lysine 5,6-aminomutase alpha subunit
K18011  beta-lysine 5,6-aminomutase beta subunit
Genes
RFR: Rfer_3887 Rfer_3888
AZA: AZKH_1576 AZKH_1577
AZI: AzCIB_1068 AzCIB_1069
ADE: Adeh_1483 Adeh_1485
ACP: A2cp1_2470 A2cp1_2472
AFW: Anae109_2347 Anae109_2349
ANK: AnaeK_2382 AnaeK_2384
MXA: MXAN_4386(kamE) MXAN_4388(kamD)
MFU: LILAB_30020 LILAB_30030
MSD: MYSTI_04875 MYSTI_04877
CCX: COCOR_03525(kamD) COCOR_03527(kamE)
SUR: STAUR_4746(kamE) STAUR_4748(kamD)
SCL: sce2889(kamD) sce2891(kamE)
CPAT: CLPA_c31440(kamE) CLPA_c31450(kamD)
CPAE: CPAST_c31440(kamE) CPAST_c31450(kamD)
CST: CLOST_1378(kamE) CLOST_1379(kamD)
STH: STH37 STH38
MBJ: KQ51_00865(kamD) KQ51_00866(kamE)
TCU: Tcur_2347
ASE: ACPL_2802(kamE) ACPL_2803
ACTN: L083_3927 L083_3928(kamE)
PGI: PG_1073(kamD) PG_1074(kamE)
PGT: PGTDC60_1134(kamE) PGTDC60_1135(kamD)
CACI: CLOAM1503(kamE) CLOAM1504(kamD)
 » 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 28:920-6 (1967)
DOI:10.1016/0006-291X(67)90067-8
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 125:226-39 (1968)
DOI:10.1016/0003-9861(68)90657-7
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 9:4890-900 (1970)
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 61:2989-2998 (1978)
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 275:106-14 (2000)
DOI:10.1074/jbc.275.1.106
  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 41:8767-76 (2002)
DOI:10.1021/bi020255k
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 48:8151-60 (2009)
DOI:10.1021/bi900828f
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 101:15870-5 (2004)
DOI:10.1073/pnas.0407074101
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 5.4.3.3
IUBMB Enzyme Nomenclature: 5.4.3.3
ExPASy - ENZYME nomenclature database: 5.4.3.3
BRENDA, the Enzyme Database: 5.4.3.3
CAS: 9075-69-8

DBGET integrated database retrieval system