KEGG   ENZYME: 5.4.3.3Help
Entry
EC 5.4.3.3                  Enzyme                                 

Name beta-lysine 5,6-aminomutase;
beta-lysine mutase;
L-beta-lysine 5,6-aminomutase
Class Isomerases;
Intramolecular transferases;
Transferring amino groups
BRITE hierarchy
Sysname (3S)-3,6-diaminohexanoate 5,6-aminomutase
Reaction(IUBMB) (3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate [RN:R03275]
Reaction(KEGG) R03275
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Substrate (3S)-3,6-diaminohexanoate [CPD:C01142]
Product (3S,5S)-3,5-diaminohexanoate [CPD:C01186]
Cofactor Cobamide coenzyme [CPD:C00194]
Comment Requires a cobamide coenzyme.
Pathway PATH: ec00310  Lysine degradation
Orthology KO: K01844  beta-lysine 5,6-aminomutase
Genes RFR: Rfer_3887 Rfer_3888
ADE: Adeh_1483 Adeh_1485
AMT: Amet_4548 Amet_4549
STH: STH37 STH38
TTE: TTE0726 TTE0727
NCA: Noca_2663 Noca_2664
STP: Strop_2265 Strop_2266
PGI: PG1073(kamD) PG1074(kamE)
FNU: FN1862 FN1863
Taxonomy
Structures PDB: 1XRS  
Reference
  Authors
  Title

  Journal
1
Retey, J., Kunz, F., Arigoni, D. and Stadtman, T.C.
Zur Kenntnis der beta-Lysin-Mutase-Reaktion: mechanismus und
sterischer Verlauf.
Helv. Chim. Acta 61 (1978) 2989-2998.
Reference
  Authors
  Title

  Journal
  Organism
2  [PMID:5649516]
Stadtman TC, Renz P.
Anaerobic degradation of lysine. V. Some properties of the cobamide
coenzyme-dependent beta-lysine mutase of Clostridium sticklandii.
Arch. Biochem. Biophys. 125 (1968) 226-39.
Clostridium sticklandii
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

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