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beta-chloro-L-alanine
NH3 + pyruvate + chloride
D-cysteine + H2O
sulfide + NH3 + pyruvate
L-cysteine sulfinic acid + reduced acceptor
SO2 + L-alanine + acceptor
L-selenocysteine + reduced acceptor
L-alanine + selenium + acceptor
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
selenomethionine reduced acceptor
methylselenole + selenide
additional information
?
-
beta-chloro-L-alanine
NH3 + pyruvate + chloride
-
alpha,beta elimination, irreversible inactivation of enzyme during the course of reaction
-
?
beta-chloro-L-alanine
NH3 + pyruvate + chloride
-
alpha,beta elimination, irreversible inactivation of enzyme during the course of reaction
-
?
beta-chloro-L-alanine
NH3 + pyruvate + chloride
-
alpha,beta elimination, irreversible inactivation of enzyme during the course of reaction
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
L-cysteine sulfinic acid + reduced acceptor
SO2 + L-alanine + acceptor
-
-
-
-
?
L-cysteine sulfinic acid + reduced acceptor
SO2 + L-alanine + acceptor
-
approx. 15% of activity with L-selenocysteine
-
?
L-cysteine sulfinic acid + reduced acceptor
SO2 + L-alanine + acceptor
-
-
-
?
L-cysteine sulfinic acid + reduced acceptor
SO2 + L-alanine + acceptor
less than 10% of activity
-
-
?
L-selenocysteine + reduced acceptor
L-alanine + selenium + acceptor
the enzyme also shows cysteine desulfurase activity, that is 280fold lower than its selenocysteine lyase activity
-
-
?
L-selenocysteine + reduced acceptor
L-alanine + selenium + acceptor
the enzyme also shows cysteine desulfurase activity, that is 280fold lower than its selenocysteine lyase activity
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
the NifS-like domain of molybdenum cofactor sulfurase ABA3 also exhibits selenocysteine lyase activity, although L-selenocysteine is unlikely to be a natural substrate
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
strictly specific, no activity with D-isomer, enzyme is inativated during course of reaction, inactivation can be prevented by addition of alpha-keto acids
formation of H2Se by nonenzymatic reduction of elemental selenium in presence of dithiothreitol
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
enzyme bound pyridoxal 5'-phosphate serves as acceptor
formation of H2Se by nonenzymatic reduction of elemental selenium in presence of dithiothreitol
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
enzyme bound pyridoxal 5'-phosphate serves as acceptor
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
enzyme bound pyridoxal 5'-phosphate serves as acceptor
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
enzyme bound pyridoxal 5'-phosphate serves as acceptor
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
three different reaction schemes suggested
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
probably functions as selenide delivery system
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
H2Se detected as product
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
probably functions as selenide delivery system
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
most likely metabolizes small amounts of selenocysteine in tissue
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
H2Se detected as product
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
H2Se detected as product
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
enzyme bound pyridoxal 5'-phosphate serves as acceptor
enzyme bound pyridoxamine 5'-phosphate formed during reaction, regeneration of enzyme by addition of an alpha-keto acid, formation of H2Se by nonenzymatic reduction of elemental selenium in presence of dithiothreitol
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
enzyme is inativated during course of reaction without addition of pyridoxal 5'-phosphate
enzyme bound pyridoxamine 5'-phosphate formed during reaction, regeneration of enzyme by addition of an alpha-keto acid, formation of H2Se by nonenzymatic reduction of elemental selenium in presence of dithiothreitol
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
probably functions as selenide delivery system
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
most likely metabolizes small amounts of selenocysteine in tissue
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
most likely metabolizes small amounts of selenocysteine in tissue
-
?
selenomethionine reduced acceptor
methylselenole + selenide
-
only the 76Se selenomethionine and not 77Se selenomethionine is used as substrate in liver homogenates
-
-
?
selenomethionine reduced acceptor
methylselenole + selenide
-
only the 76Se selenomethionine and not 77Se selenomethionine is used as substrate in liver homogenates
-
-
?
additional information
?
-
-
no activity with L-cysteine
-
-
?
additional information
?
-
-
no activity with L-cysteine
-
-
?
additional information
?
-
-
traces of activity with L-cysteine
-
-
?
additional information
?
-
-
traces of activity with L-cysteine
-
-
?
additional information
?
-
-
traces of activity with L-cysteine, L-selenocystine, L-cystine and L-aspartic acid
-
-
?
additional information
?
-
the enzyme is involved in Fe-S cluster assembly in haloarchaea
-
-
?
additional information
?
-
the enzyme is involved in Fe-S cluster assembly in haloarchaea
-
-
?
additional information
?
-
-
the enzyme is specific for L-selenocysteine versus L-cysteine on a molecular level, no activity with L-cysteine
-
-
?
additional information
?
-
the enzyme is specific for L-selenocysteine versus L-cysteine, substrate specificity for selenium and sulfur is determined by a single residue, Asp246, in human selenocysteine lyase
-
-
?
additional information
?
-
-
the enzyme is specific for L-selenocysteine versus L-cysteine, substrate specificity for selenium and sulfur is determined by a single residue, Asp246, in human selenocysteine lyase
-
-
?
additional information
?
-
the enzyme is specific for L-selenocysteine versus L-cysteine, substrate specificity for selenium and sulfur is determined by a single residue, Asp246, in human selenocysteine lyase, chemical basis for and mechanism of the enzyme's substrate discrimination of wild-type enzyme and mutant D146K/H389T, overview. The wild-type reaction with Cys is a single-turnover reaction, producing a dead-end protein adduct
-
-
?
additional information
?
-
-
the enzyme is specific for L-selenocysteine versus L-cysteine, substrate specificity for selenium and sulfur is determined by a single residue, Asp246, in human selenocysteine lyase, chemical basis for and mechanism of the enzyme's substrate discrimination of wild-type enzyme and mutant D146K/H389T, overview. The wild-type reaction with Cys is a single-turnover reaction, producing a dead-end protein adduct
-
-
?
additional information
?
-
-
the enzyme catalyzes the elimination of an elemental form of selenium from free selenocysteine and delivers this selenium directly to selenophosphate synthetase
-
-
?
additional information
?
-
traces of activity with L-cysteine
-
-
?
additional information
?
-
-
traces of activity with L-cysteine
-
-
?
additional information
?
-
traces of activity with L-cysteine
-
-
?
additional information
?
-
-
traces of activity with L-cysteine
-
-
?
additional information
?
-
-
the enzyme is specific for L-selenocysteine versus L-cysteine on a molecular level, no activity with L-cysteine
-
-
?
additional information
?
-
-
the enzyme is specific for L-selenocysteine versus L-cysteine on a molecular level, no activity with L-cysteine
-
-
?
additional information
?
-
-
the enzyme is specific for L-selenocysteine versus L-cysteine on a molecular level, no activity with L-cysteine. Residue Cys375 sorts selenium from cysteine and directs it to the active site
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
no activity with L-cysteine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
additional information
?
-
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
probably functions as selenide delivery system
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
probably functions as selenide delivery system
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
most likely metabolizes small amounts of selenocysteine in tissue
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
probably functions as selenide delivery system
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
most likely metabolizes small amounts of selenocysteine in tissue
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
-
most likely metabolizes small amounts of selenocysteine in tissue
-
?
additional information
?
-
the enzyme is involved in Fe-S cluster assembly in haloarchaea
-
-
?
additional information
?
-
the enzyme is involved in Fe-S cluster assembly in haloarchaea
-
-
?
additional information
?
-
-
the enzyme catalyzes the elimination of an elemental form of selenium from free selenocysteine and delivers this selenium directly to selenophosphate synthetase
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Mihara, H.; Fujii, T.; Kato, S.; Kurihara, T.; Hata, Y.; Esaki, N.
Structure of external aldimine of Escherichia coli CsdB, an IscS/NifS homolog: implications for its specificity toward selenocysteine
J. Biochem.
131
679-685
2002
Escherichia coli
brenda
Mihara, H.; Kurihara, T.; Yoshimura, T.; Esaki, N.
Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions
J. Biochem.
127
559-567
2000
Escherichia coli
brenda
Esaki, N.; Nakamura, T.; Tanaka, H.; Soda, K.
Selenocysteine lyase, a novel enzyme that specifically acts on selenocysteine
J. Biol. Chem.
257
4386-4391
1982
Bos taurus, Canis lupus familiaris, Cavia porcellus, Oryctolagus cuniculus, Felis catus, Platyrrhini, Mus musculus, Rattus norvegicus, Sus scrofa
brenda
Chocat, P.; Esaki, N.; Tanizawa, K.; Nakamura, T.; Tanaka, H.; Soda, K.
Purification and characterization of selenocysteine beta-lyase from Citrobacter freundii
J. Bacteriol.
163
669-676
1985
Citrobacter freundii
brenda
Esaki, N.; Karai, N.; Nakamura, T.; Tanaka, H.; Soda, K.
Mechanism of reactions catalyzed by selenocysteine beta-lyase
Arch. Biochem. Biophys.
238
418-423
1985
Sus scrofa
brenda
Esaki, N.; Soda, K.
Selenocysteine beta-lyase from Citrobacter freundii
Methods Enzymol.
143
493-496
1987
Citrobacter freundii, Citrobacter freundii IRC 0070
-
brenda
Esaki, N.; Soda, K.
Selenocysteine beta-lyase (porcine)
Methods Enzymol.
143
415-418
1987
Sus scrofa
brenda
Daher, R.; Van Lente, F.
Characterization of selenocysteine lyase in human tissues and its relationship to tissue selenium concentrations
J. Trace Elem. Electrolytes Health Dis.
6
189-194
1992
Homo sapiens, Sus scrofa
brenda
Mihara, H.; Maeda, M.; Fujii, T.; Kurihara, T.; Hata, Y.; Esaki, N.
A nifS-like gene, csdB, encodes an Escherichia coli counterpart of mammalian selenocysteine lyase. Gene cloning, purification, characterization and preliminary X-ray crystallographic studies
J. Biol. Chem.
274
14768-14772
1999
Escherichia coli
brenda
Mihara, H.; Kurihara, T.; Watanabe, T.; Yoshimura, T.; Esaki, N.
cDNA cloning, purification, and characterization of mouse liver selenocysteine lyase. Candidate for selenium delivery protein in selenoprotein synthesis
J. Biol. Chem.
275
6195-6200
2000
Sus scrofa, Mus musculus (Q9JLI6), Mus musculus
brenda
Fujii, T.; Maeda, M.; Mihara, H.; Kurihara, T.; Esaki, N.; Hata, Y.
Structure of a NifS homologue: X-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyase
Biochemistry
39
1263-1273
2000
Escherichia coli (P77444), Escherichia coli
brenda
Mihara, H.; Esaki, N.
Selenocysteine lyase from mouse liver
Methods Enzymol.
347
198-203
2002
Mus musculus (Q9JLI6), Mus musculus
brenda
Garifullina, G.F.; Owen, J.D.; Lindblom, S.D.; Tufan, H.; Pilon, M.; Pilon-Smits, E.A.H.
Expression of a mouse selenocysteine lyase in Brassica juncea chloroplasts affects selenium tolerance and accumulation
Physiol. Plant.
118
538-544
2003
Mus musculus
-
brenda
Pilon, M.; Owen, J.D.; Garifullina, G.F.; Kurihara, T.; Mihara, H.; Esaki, N.; Pilon-Smits, E.A.
Enhanced selenium tolerance and accumulation in transgenic Arabidopsis expressing a mouse selenocysteine lyase
Plant Physiol.
131
1250-1257
2003
Mus musculus
brenda
Kurokawa, S.; Mihara, H.; Kurihara, T.; Esaki, N.
Expression analysis of mammalian selenocysteine lyase
Biomed. Res. Trace Elements
15
278-280
2004
Mus musculus, Mus musculus C57BL/6
-
brenda
Stadtman, T.
Methanococcus vannielii selenium metabolism: purification and N-terminal amino acid sequences of a novel selenium-binding protein and selenocysteine lyase
IUBMB Life
56
427-431
2004
Methanococcus vannielii
brenda
Heidenreich, T.; Wollers, S.; Mendel, R.R.; Bittner, F.
Characterization of the NifS-like domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration
J. Biol. Chem.
280
4213-4218
2005
Arabidopsis thaliana
brenda
Suzuki, K.T.; Kurasaki, K.; Suzuki, N.
Selenocysteine beta-lyase and methylselenol demethylase in the metabolism of Se-methylated selenocompounds into selenide
Biochim. Biophys. Acta
1770
1053-1061
2007
Rattus norvegicus, Rattus norvegicus Wistar
brenda
Jafari, C.; Panzer, U.; Steinmetz, O.M.; Zahner, G.; Stahl, R.A.; Harendza, S.
Enhanced expression of selenocysteine lyase in acute glomerulonephritis and its regulation by AP-1
Cell. Mol. Biol. Lett.
11
424-437
2006
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Banuelos, G.; LeDuc, D.L.; Pilon-Smits, E.A.; Terry, N.
Transgenic Indian mustard overexpressing selenocysteine lyase or selenocysteine methyltransferase exhibit enhanced potential for selenium phytoremediation under field conditions
Environ. Sci. Technol.
41
599-605
2007
Brassica juncea
brenda
Tobe, R.; Mihara, H.; Kurihara, T.; Esaki, N.
Identification of proteins interacting with selenocysteine lyase
Biosci. Biotechnol. Biochem.
73
1230-1232
2009
Mus musculus
brenda
Poliak, P.; Van Hoewyk, D.; Obornik, M.; Zikova, A.; Stuart, K.D.; Tachezy, J.; Pilon, M.; Lukes, J.
Functions and cellular localization of cysteine desulfurase and selenocysteine lyase in Trypanosoma brucei
FEBS J.
277
383-393
2010
Trypanosoma brucei
brenda
Omi, R.; Kurokawa, S.; Mihara, H.; Hayashi, H.; Goto, M.; Miyahara, I.; Kurihara, T.; Hirotsu, K.; Esaki, N.
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Homo sapiens (Q96I15), Homo sapiens
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Homo sapiens (Q96I15), Homo sapiens
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Mus musculus (Q9JLI6)
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