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4.4.1.8 c |
Activity |
4.4.1.8 |
Description |
Cystathionine beta-lyase (family c) |
Notes |
A family composed by eukaryotic sequences (from planta and fungi) closely related to cystathionine gamma-lyases (family 4.4.1.1). |
PDB |
1IBJ; |
PLP Fold Type |
I |
PLP-dependent Domain |
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Number of sequences |
15 |
Sequences in seed alignment |
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Reference sequence |
METC_ARATH |
Domain interval |
88-460 |
Catalytic site |
278 K |
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References |
Oogai S, Fukuta M, Watanabe K, Inafuku M, Oku H (2019) Molecular characterization of mimosinase and cystathionine β-lyase in the Mimosoideae subfamily member Mimosa pudica J Plant Res 132 667-680. Holt S, Cordente AG, Williams SJ, Capone DL, Jitjaroen W, Menz IR, Curtin C, Anderson PA. (2011) Engineering Saccharomyces cerevisiae to release 3-Mercaptohexan-1-ol during fermentation through overexpression of an S. cerevisiae Gene, STR3, for improvement of wine aroma Appl Environ Microbiol 77 3626-32. Gidijala L, van der Klei IJ, Veenhuis M, Kiel JA. (2007) Reprogramming Hansenula polymorpha for penicillin production: expression of the Penicillium chrysogenum pcl gene FEMS Yeast Res 7 1160-7. Breitinger, U.; Clausen, T.; Ehlert, S.; Huber, R.; Laber, B.; Schmidt, F.; Pohl, E.; Messerschmidt, A. (2001) The three-dimensional structure of cystathionine beta-lyase from Arabidopsis and its substrate specificity Plant Physiol 126 631-42. Sienko, M.; Paszewski, A. (1999) The metG gene of Aspergillus nidulans encoding cystathionine beta-lyase: cloning and analysis Curr Genet 35 638-46. Ravanel, S.; Job, D.; Douce, R. (1996) Purification and properties of cystathionine beta-lyase from Arabidopsis thaliana overexpressed in Escherichia coli Biochem J 320 383-92. Articles on 4.4.1.8.c |
last changed |
2008/04/14 19:33 |
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