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4.1.1.96 |
Activity |
4.1.1.96 |
Description |
Carboxynorspermidine decarboxylase |
Notes |
Family composed of bacterial fold-type III enzymes, distantly related to Diaminopimelate decarboxylase (EC 4.1.1.20). |
PDB |
3N29; |
PLP Fold Type |
III |
PLP-dependent Domain |
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Number of sequences |
16 |
Sequences in seed alignment |
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Reference sequence |
BAA06561 |
Domain interval |
14-244 |
Catalytic site |
41 K |
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References |
Deng X, Lee J, Michael AJ, Tomchick DR, Goldsmith EJ, Phillips MA. (2010) Evolution of substrate specificity within a diverse family of beta/alpha-barrel-fold basic amino acid decarboxylases: X-ray structure determination of enzymes with specificity for L-arginine and carboxynorspermidine. J Biol Chem. 285 25708-19. Lee J, Sperandio V, Frantz DE, Longgood J, Camilli A, Phillips MA, Michael AJ. (2009) An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae J Biol Chem 284 9899-907. Yamamoto S, Sugahara T, Tougou K, Shinoda S. (1994) Cloning and nucleotide sequence of the carboxynorspermidine decarboxylase gene from Vibrio alginolyticus Microbiology 140 3117-24. Articles on 4.1.1.96 |
last changed |
2018/05/08 08:54 |
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