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B6db families:
Description Cystathionine gamma-lyase
Notes Rather compact family, but strictly related to other families catalyzing transsulfuration reactions.
Indeed, the enzymes included in this family may also exhibit gamma-synthase activity (EC
The enzyme from Lactococcus lactis can carry out both an alpha,gamma-elimination and an alpha,beta-elimination reactions on cystathionine, hence in some database entries this gene product is classified as cystathionine beta-lyase (EC
PLP Fold Type I
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type I

Number of sequences 34
Sequences in seed alignment
BacteriaCAE81155 (Bdellovibrio bacteriovorus); AAX99219 (Helicobacter pylori ); ACA49848 (Lactobacillus casei); F83595 (Pseudomonas aeruginosa ); NP_927875 (Photorhabdus luminescens); YP_811264 (Oenococcus oeni); CAC05298 (Lactobacillus reuteri); AAF36088 (Lactococcus lactis); ZP_00036934 (Enterococcus faecium); WP_011257665 (Xanthomonas oryzae pv. oryzae); CAA17195 (Mycobacterium tuberculosis); AAB86866 (Stenotrophomonas maltophilia); NP_105358 (Mesorhizobium loti); AAO80153 (Enterococcus faecalis);
FungiCYS3_YEAST (Saccharomyces cerevisiae); AAF97598 (Acremonium chrysogenum); AAK94040 (Neurospora crassa); EAA51463 (Magnaporthe grisea); EAA68643 (Gibberella zeae);
MetazoaCGL_MOUSE (Mus musculus); AAH56538 (Danio rerio); CGL_RAT (Rattus norvegicus); AAH61381 (Xenopus tropicalis); NP_611352 (Drosophila melanogaster); CGL_HUMAN (Homo sapiens); CGL_CAEEL (Caenorhabditis elegans); EAA05138 (Anopheles gambiae str. PEST); CAE56905 (Caenorhabditis briggsae); NP_507053 (Caenorhabditis elegans);
Other_EukaryaEPT25975 (Toxoplasma gondii); XP_011130343 (Gregarina niphandrodes); PHJ19884 (Cystoisospora suis); XP_003879319 (Leishmania mexicana); EKG0314 (Trypanosoma cruzi);

DISPLAY: Fasta format, alignment, hmm, hmm_local

Reference sequence CGL_RAT
Domain interval 18-394
Catalytic site 211 K
 Maresi E, Janson G, Fruncillo S, Paiardini A, Vallone R, Dominici P, Astegno A (2018) Functional Characterization and Structure-Guided Mutational Analysis of the Transsulfuration Enzyme Cystathionine γ-Lyase from Toxoplasma gondii Int J Mol Sci 19 E2111.

 Ngo HP, Cerqueira NM, Kim JK, Hong MK, Fernandes PA, Ramos MJ3, Kang LW (2014) PLP undergoes conformational changes during the course of an enzymatic reaction Acta Crystallogr D Biol Crystallogr 70 596-606.

 Wang JC, Temuujin U, Kim JG, Park YJ, Lee B-M, Chioi CS, Silo-Sun LA, Kang HW (2011) Functional analysis and expressional regulation of wxoE and wxoF in lipopolysaccharide (lps) biosynthesis gene cluster I of Xanthomonas oryzae pv. oryzae Physiol Mol Plant Pathol 75 129–136.

 Knoll C, du Toit M, Schnell S, Rauhut D, Irmler S (2010) Cloning and characterisation of a cystathionine beta/gamma-lyase from two Oenococcus oeni oenological strains Appl Microbiol Biotechnol 89 1051-60.

 Irmler S, Schäfer H, Beisert B, Rauhut D, Berthoud H. (2009) Identification and characterization of a strain-dependent cystathionine beta/gamma-lyase in Lactobacillus casei potentially involved in cysteine biosynthesis. FEMS Microbiol Lett. 295 67-76.

 Kong Y, Wu D, Bai H, Han C, Chen J, Chen L, Hu L, Jiang H, Shen X. (2008) Enzymatic characterization and inhibitor discovery of a new cystathionine {gamma}-synthase from Helicobacter pylori J Biochem 143 59-68.

 Wheeler PR, Coldham NG, Keating L, Gordon SV, Wooff EE, Parish T, Hewinson RG. (2005) Functional demonstration of reverse transsulfuration in the Mycobacterium tuberculosis complex reveals that methionine is the preferred sulfur source for pathogenic Mycobacteria J Biol Chem 280 8069-78.

 Messerschmidt, A. Worbs, M. Steegborn, C. Wahl, M.C. Huber, R. Laber, B. Clausen, T. (2003) Determinants of enzymatic specificity in the Cys-Met-metabolism PLP-dependent enzymes family: crystal structure of cystathionine gamma-lyase from yeast and intrafamiliar structure comparison Biol Chem 384 373-386.

 De Angelis, M.; Curtin, A. C.; McSweeney, P. L.; Faccia, M.; Gobbetti, M. (2002) Lactobacillus reuteri DSM 20016: purification and characterization of a cystathionine gamma-lyase and use as adjunct starter in cheesemaking J Dairy Res 69 255-67.

 Marcos, A.T.; Kosalkova, K.; Cardoza, R.E.; Fierro, F.; Gutierrez, S.; Martin, J.F. (2001) Characterization of the reverse transsulfuration gene mecB of Acremonium chrysogenum, which encodes a functional cystathionine-gamma-lyase Mol Gen Genet 264 746-54.

 Dobric, N. Limsowtin, G.K. Hillier, A.J. Dudman N.P. Davidson, B.E. (2000) Identification and characterization of a cystathionine beta/gamma-lyase from Lactococcus lactis ssp. cremoris MG1363 FEMS Microbiol Lett. 182 249-254.

 Ono, B.; Ishii, N.; Naito, K.; Miyoshi, S.; Shinoda, S.; Yamamoto, S.; Ohmori, S. (1993) Cystathionine gamma-lyase of Saccharomyces cerevisiae: structural gene and cystathionine gamma-synthase activity Yeast 9 389-97.

 Lu, Y.; O'Dowd, B. F.; Orrego, H.; Israel, Y. (1992) Cloning and nucleotide sequence of human liver cDNA encoding for cystathionine gamma-lyase Biochem Biophys Res Commun 189 749-58.

 Erickson, P. F.; Maxwell, I. H.; Su, L. J.; Baumann, M.; Glode, L. M. (1990) Sequence of cDNA for rat cystathionine gamma-lyase and comparison of deduced amino acid sequence with related Escherichia coli enzymes Biochem J 269 335-40.

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last changed 2014/02/26 10:34

B6db families