B6db families : 4_4_1

	Activities \| Families \| Sequences \| Fold types \| References \| Help

4.4.1.1

Activity

4.4.1.1

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 2.5.1.48).
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 4.1.4.8)

PDB

1N8P;

PLP Fold Type

PLP-dependent Domain

Domain alignment
Domain hmm

Fold type I

Number of sequences

Sequences in seed alignment

Bacteria	AAD07176 (Helicobacter pylori ); CAE81155 (Bdellovibrio bacteriovorus); AAB86866.1 (Stenotrophomonas maltophilia); AAF36088 (Lactococcus lactis); F83595 (Pseudomonas aeruginosa ); NP_105358 (Mesorhizobium loti); CAC05298 (Lactobacillus reuteri); NP_927875 (Photorhabdus luminescens); CAA17195 (Mycobacterium tuberculosis); AAO80153 (Enterococcus faecalis); ZP_00036934 (Enterococcus faecium); AAM38445 (Xanthomonas axonopodis);
Fungi	EAA51463 (Magnaporthe grisea); CYS3_YEAST (Saccharomyces cerevisiae); AAK94040.1 (Neurospora crassa); EAA68643 (Gibberella zeae); AAF97598.1 (Acremonium chrysogenum);
Metazoa	CGL_HUMAN (Homo sapiens); NP_507053.1 (Caenorhabditis elegans); AAH56538.1 (Danio rerio); NP_611352.1 (Drosophila melanogaster); CGL_CAEEL (Caenorhabditis elegans); CAE56905 (Caenorhabditis briggsae); CGL_MOUSE (Mus musculus); EAA05138.1 (Anopheles gambiae str. PEST); AAH61381 (Xenopus tropicalis); CGL_RAT (Rattus norvegicus);

DISPLAY: Fasta format, alignment, hmm, hmm_local

Reference sequence

CGL_RAT

Domain interval

18-394

Catalytic site

211 K

References

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..

Articles on 4.4.1.1

last changed

2008/04/02 19:37