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B6db activities: 4.4.1.28

4.4.1.28
Description L-cysteine desulfidase
Alternative names L-cysteine desulfhydrase;
cystalysin;
C-S lyase (ambiguous).
Catalyzed reaction L-Cysteine + H(2)O = pyruvate + H(2)S + NH(3)
Cofactor Pyridoxal-phosphate or [4Fe-4S] cluster.
Comments It cleaves a carbon-sulfur bound releasing sulfide and the unstable enamine product 2-aminoprop-2-enoate that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The reaction can be catalysed by other pyridoxal-phosphate proteins (cf. EC 4.4.1.1, cystathionine γ-lyase).
The enzyme from the archaeon Methanocaldococcus jannaschii contains a [4Fe-4S] cluster instead of PLP.
The validated PLP-dependent enzymes that catalyze this reaction also show cystathionine beta-lyase activity (E.C. 4.4.1.8) and sometimes methionine gamma-lyase activity (4.4.1.11).
PDB 1C7O;
Organisms -Eubacteria -Archea
 

Family 

 
Links Enzyme (activities) 4.4.1.28
BRENDA (activities) 4.4.1.28
KEGG (pathways) 4.4.1.28
PLPMDB (PLP mutants) 4.4.1.28
 
References
  Allegrini A, Astegno A, La Verde V, Dominici P. (2017) Characterization of C-S lyase from Lactobacillus delbrueckii subsp. bulgaricus ATCC BAA-365 and its potential role in food flavour applications J Biochem 161 49-360.

 Takumi, K.; Nonaka, G. (2016) Bacterial Cysteine-Inducible Cysteine Resistance Systems J Bacteriol 198 1384-92.

 Santiago M, Gardner RC (2015) The IRC7 gene encodes cysteine desulphydrase activity and confers on yeast the ability to grow on cysteine as a nitrogen source Yeast 32 519-32.

 Xie Y, Lai D, Mao Y, Zhang W, Shen W, Guan R. (2013) Molecular cloning, characterization, and expression analysis of a novel gene encoding L-cysteine desulfhydrase from Brassica napus. Mol Biotechnol. 54 737-46.

 Oguri T1, Schneider B, Reitzer L. (2012) Cysteine catabolism and cysteine desulfhydrase (CdsH/STM0458) in Salmonella enterica serovar typhimurium J Bacteriol 194 4366-76.

 Alvarez C, Calo L, Romero LC, García I, Gotor C. (2010) An O-acetylserine(thiol)lyase homolog with L-cysteine desulfhydrase activity regulates cysteine homeostasis in Arabidopsis Plant Physiol 152 656-69.

 Yano T, Fukamachi H, Yamamoto M, Igarashi T. (2009) Characterization of L-cysteine desulfhydrase from Prevotella intermedia Oral Microbiol Immunol 24 485-92.

 Martínez-Cuesta MC, Peláez C, Eagles J, Gasson MJ, Requena T, Hanniffy SB. (2006) YtjE from Lactococcus lactis IL1403 Is a C-S lyase with alpha, gamma-elimination activity toward methionine. Appl Environ Microbiol 72 4878-84.

 Auger, S.; Gomez, M.P.; Danchin, A.; Martin-Verstraete, I. (2005) The PatB protein of Bacillus subtilis is a C-S-lyase Biochimie 87 231-238.

 Fukamachi, H.; Nakano, Y.; Yoshimura, M.; Koga, T. (2002) Cloning and characterization of the L-cysteine desulfhydrase gene of Fusobacterium nucleatum FEMS Microbiol Lett 215 75-80.

 Wada, M., Awano, N., Haisa, K., Takagi, H., Nakamori, S. (2002) Purification, characterization and identification of cysteine desulfhydrase of Corynebacterium glutamicum, and its relationship to cysteine production FEMS Microbiol Lett 217 103-107.

 Krupka HI, Huber R, Holt SC, Clausen T. (2000) Crystal structure of cystalysin from Treponema denticola: a pyridoxal 5'-phosphate-dependent protein acting as a haemolytic enzyme EMBO J 19 3168-78.

 Chu, L.; Ebersole, J. L.; Kurzban, G. P.; Holt, S. C. (1999) Cystalysin, a 46-kDa L-cysteine desulfhydrase from Treponema denticola: biochemical and biophysical characterization Clin Infect Dis 28 442-50.

 Rossol, I.; Puhler, A. (1992) The Corynebacterium glutamicum aecD gene encodes a C-S lyase with alpha, beta-elimination activity that degrades aminoethylcysteine J Bacteriol 174 2968-77.

Articles on 4.4.1.28
 
last changed 2019/06/20 13:29

B6db activities