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Information on EC 4.4.1.16 - selenocysteine lyase and Organism(s) Escherichia coli and UniProt Accession P77444

for references in articles please use BRENDA:EC4.4.1.16
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IUBMB Comments
A pyridoxal-phosphate protein. Dithiothreitol or 2-sulfanylethan-1-ol (2-mercaptoethanol) can act as the reducing agent in the reaction. The enzyme from animals does not act on cysteine, serine or chloroalanine [1,3], while the enzyme from bacteria shows activity with cysteine (cf. EC 2.8.1.7, cysteine desulfurase) .
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This record set is specific for:
Escherichia coli
UNIPROT: P77444
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
scl, selenocysteine lyase, selenocysteine beta-lyase, sec lyase, aba3-nifs, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SCL
-
-
-
-
selenocysteine beta-lyase
-
-
-
-
selenocysteine lyase
-
-
selenocysteine reductase
-
-
-
-
additional information
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha,beta-elimination
-
-
-
-
elimination of H2Se
-
-
-
-
cleavage of C-Se bond
-
-
-
-
elimination of SO2
-
-
-
-
oxidative elimination of NH3
-
-
-
-
elimination of chloride
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
L-selenocysteine selenide-lyase (L-alanine-forming)
A pyridoxal-phosphate protein. Dithiothreitol or 2-sulfanylethan-1-ol (2-mercaptoethanol) can act as the reducing agent in the reaction. The enzyme from animals does not act on cysteine, serine or chloroalanine [1,3], while the enzyme from bacteria shows activity with cysteine (cf. EC 2.8.1.7, cysteine desulfurase) [2].
CAS REGISTRY NUMBER
COMMENTARY hide
82047-76-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
show the reaction diagram
L-cysteine sulfinic acid + reduced acceptor
SO2 + L-alanine + acceptor
show the reaction diagram
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
show the reaction diagram
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
required
pyridoxal 5'-phosphate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyruvate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
30
L-cysteine sulfinate
-
in the presence of pyruvate, pH 7.5
2.6
L-selenocysteine
-
in the presence of pyruvate, pH 7.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6
-
purified enzyme, pH 7.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
the enzyme is involved in selenocysteine biosynthesis. The interaction between selenocysteine lyase and selenophosphate synthetase occurs with a stoichiometry of 1:1
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
-
SDS-PAGE
44440
-
calculated from amino acid sequence
88000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
crystal structure analysis
dimer
-
2 * 43000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method
hanging drop vapor diffusion method
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C364A
-
increased activity towards L-selenocysteine and L-cysteine sulfinate, activity toward L-cysteine was completely abolished
H123A
-
only 1% of activity remaining compared to wild type, contributes to stabilization of pyridoxal 5'-phospahte
H55A
-
no effect on activity
R379A
-
less than 1% of activity remaining compared to wild type
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpressed protein
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli JM109
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Scortecci, J.F.; Serrao, V.H.B.; Fernandes, A.F.; Basso, L.G.M.; Gutierrez, R.F.; Araujo, A.P.U.; Neto, M.O.; Thiemann, O.H.
Initial steps in selenocysteine biosynthesis The interaction between selenocysteine lyase and selenophosphate synthetase
Int. J. Biol. Macromol.
156
18-26
2020
Escherichia coli
Manually annotated by BRENDA team