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5.4.3.4 |
Description |
D-lysine 5,6-aminomutase |
Alternative names |
D-alpha-lysine mutase. |
Catalyzed reaction |
D-lysine = 2,5-diaminohexanoate. |
Cofactor |
Cobalamin. Pyridoxal-phosphate. |
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EC 5.4.3.4 includes EC 5.4.3.3 |
PDB |
1XRS; |
Organisms |
-Eubacteria |
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Family |
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Links |
Enzyme (activities) 5.4.3.4
BRENDA (activities) 5.4.3.4
KEGG (pathways) 5.4.3.4
PLPMDB (PLP mutants) 5.4.3.4
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References |
Tseng CH, Yang CH, Lin HJ, Wu C, Chen HP. (2007) The S subunit of D-ornithine aminomutase from Clostridium sticklandii is responsible for the allosteric regulation in D-alpha-lysine aminomutase FEMS Microbiol Lett 274 148-53. Berkovitch, F.; Behshad, E.; Tang, K.H.; Enns, E.A.; Frey, P.A.; Drennan, C.L.
(2004) 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 U S A 101 15870-5. Tang, K. H.; Harms, A.; Frey, P. A.
(2002) Identification of a novel pyridoxal 5'-phosphate binding site in adenosylcobalamin-dependent lysine 5,6-aminomutase from Porphyromonas gingivalis Biochemistry 41 8767-76. Chang, C. H.; Frey, P. A. (2000) Cloning, sequencing, heterologous expression, purification, and characterization of adenosylcobalamin-dependent D-lysine 5, 6-aminomutase from Clostridium sticklandii J Biol Chem 275 106-14. Articles on 5.4.3.4 |
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last changed |
2019/06/20 13:37 |
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