Cystathionine β-lyase

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Cystathionine β-lyase ( Escherichia coli )
Cystathionine β-lyase (Escherichia coli)
Tertiary structure of cystathionine-β-lyase from Escherichia coli according to PDB  1cl1
other names
  • Beta cystathionase
  • Cystine lyase
  • Cystathionine-L-homocysteine-lyase (deaminating)
  • L-cystathionine-L-homocysteine ​​lyase (deaminating)

Existing structural data : 1cl2 , 1ibj , 2gqn

Mass / length primary structure 395 amino acids , 43212 Da
Secondary to quaternary structure Homotetramer
Cofactor Pyridoxal phosphate
Identifier
Gene name (s) metC ( E. coli ), STR3 ( S. cerevisiae )
External IDs
Enzyme classification
EC, category 4.4.1.8 ,  lyases
Response type Transsulfurization
Substrate Cystathionine, water
Products Homocysteine, pyruvate, ammonia
Occurrence
Parent taxon Bacteria, yeast and plants

The cystathionine-β-lyase ( CBL ) is an enzyme from the group of lyases that in the transfer of sulfur-containing molecules ( transsulfuration ) in the amino acid metabolism is involved.

properties

Reaction of cystathionine-β-lyase (CbL) in amino acid degradation in plants

Cystathionine β-lyase is found in bacteria , yeast and plants . It catalyzes the hydrolysis of cystathionine , which produces homoserine and pyruvate with the loss of an amine . Among other things, it is involved in methionine , cysteine , selenocysteine , nitrogen and sulfur metabolism (transsulfurization). As co-factor is pyridoxal phosphate (PLP) was used. The cystathionine-β-lyase is structurally related to the cystathionine-γ-synthase . The CBL is not found in animals, which is why it is a target in antibiotic development . The plant-based CBL is somewhat larger and, in addition to cystathionine, also binds the non-proteinogenic amino acid djenkolic acid .

Individual evidence

  1. ↑ S. Holt, AG Cordente, C. Curtin: Saccharomyces cerevisiae STR3 and yeast cystathionine β-lyase enzymes: The potential for engineering increased flavor release. In: Bioengineered bugs. Volume 3, number 3, 2012 May-Jun, pp. 178-180, doi: 10.4161 / bbug.19566 , PMID 22572787 , PMC 3370937 (free full text).
  2. ↑ a b c D. Q. Nguyen, HP Ngo, YJ Ahn, SH Lee, LW Kang: Expression, crystallization and preliminary X-ray crystallographic analysis of cystathionine β-lyase from Acinetobacter baumannii OXA-23. In: Acta crystallographica. Section F, Structural biology communications. Volume 70, Pt 10 October 2014, pp. 1368-1371, doi: 10.1107 / S2053230X14017981 , PMID 25286941 .
  3. ↑ AF Jaworski, SM Aitken: Exploration of the six tryptophan residues of Escherichia coli cystathionine β-lyase as probes of enzyme conformational change. In: Archives of biochemistry and biophysics. Volume 538, number 2, October 2013, pp. 138-144, doi: 10.1016 / j.abb.2013.07.006 , PMID 23969077 .
  4. ↑ AL Manders, AF Jaworski, M. Ahmed, SM Aitken: Exploration of structure-function relationships in Escherichia coli cystathionine γ-synthase and cystathionine β-lyase via chimeric constructs and site-specific substitutions. In: Biochimica et Biophysica Acta . Volume 1834, number 6, June 2013, pp. 1044-1053, doi: 10.1016 / j.bbapap.2013.02.036 , PMID 23470500 .
  5. ↑ U. Breitinger, T. Clausen, S. Ehlert, R. Huber, B. Laber, F. Schmidt, E. Pohl, A. Messerschmidt: The three-dimensional structure of cystathionine beta-lyase from Arabidopsis and its substrate specificity. In: Plant physiology. Volume 126, Number 2, June 2001, pp. 631-642, PMID 11402193 , PMC 111155 (free full text).