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4.4.1.15 |
Activity |
4.4.1.15 |
Description |
D-cysteine desulfhydrase |
Notes |
A family of bacterial and plant enzymes, strictly related to L-cysteate sulfo-lyases (EC 4.4.1.25) and to 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7).
Ser/Thr288 and Thr315 (numbering after the reference sequence from E. coli; the corresponding residues in the Solanum lycopersicon enzyme are Ser358 and Thr386, respectively) have been described by Todorovic and Glick as distinctive residues.
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PDB |
4D9F; |
PLP Fold Type |
II |
PLP-dependent Domain |
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Number of sequences |
14 |
Sequences in seed alignment |
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Reference sequence |
DCYD_ECOLI |
Domain interval |
12-316 |
Catalytic site |
51 K |
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References |
Zhou H, Guan W, Zhou M, Shen J, Liu X, Wu D, Yin X, Xie Y (2020) Cloning and Characterization of a gene Encoding True D-cysteine Desulfhydrase from Oryza sativa Plant Mol Biol Rep 38 95–113. Ekimova GA, Fedorov DN, Tani A, Doronina NV, Trotsenko YA (2018) Distribution of 1-aminocyclopropane-1-carboxylate deaminase and D-cysteine desulfhydrase genes among type species of the genus Methylobacterium Antonie Van Leeuwenhoek 111 1723-1734. Bharath SR, Bisht S, Harijan RK, Savithri HS, Murthy MR (2012) Structural and mutational studies on substrate specificity and catalysis of Salmonella typhimurium D-cysteine desulfhydrase PLoS One 7 e36267. Todorovic B, Glick BR (2008) The interconversion of ACC deaminase and D-cysteine desulfhydrase by directed mutagenesis Planta 229 193-205. Riemenschneider, A.; Wegele, R.; Schmidt, A.; Papenbrock, J. (2005) Isolation and characterization of a D-cysteine desulfhydrase protein from Arabidopsis thaliana FEBS J 272 1291-1304. Soutourina, J.; Blanquet, S.; Plateau, P. (2001) Role of D-cysteine desulfhydrase in the adaptation of Escherichia coli to D-cysteine J Biol Chem 276 40864-72. Articles on 4.4.1.15 |
last changed |
2020/02/21 10:27 |
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