Information on EC 4.1.1.29 - Sulfinoalanine decarboxylase

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The expected taxonomic range for this enzyme is: Coelomata

EC NUMBER
COMMENTARY hide
4.1.1.29
-
RECOMMENDED NAME
GeneOntology No.
Sulfinoalanine decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-sulfino-L-alanine = hypotaurine + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
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Taurine and hypotaurine metabolism
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taurine biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
3-sulfino-L-alanine carboxy-lyase (hypotaurine-forming)
A pyridoxal-phosphate protein. Also acts on L-cysteate. The 1992 edition of the Enzyme List erroneously gave the name sulfoalanine decarboxylase to this enzyme.
CAS REGISTRY NUMBER
COMMENTARY hide
62213-10-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
no activity in Katsuwonus pelamis
no activity in liver and hepatopancreas
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Manually annotated by BRENDA team
no activity in Seriola quinqueradiata
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-
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Manually annotated by BRENDA team
no activity in Thunnus thynnus
no activity in liver and hepatopancreas
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Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-sulfino-L-alanine
hypotaurine + CO2
show the reaction diagram
-
-
-
?
Cysteic acid
2-Aminoethane sulfonate + CO2
show the reaction diagram
Cysteine sulfinate
?
show the reaction diagram
Cysteine sulfonate
?
show the reaction diagram
Glu
4-Aminobutanoate + CO2
show the reaction diagram
L-Asp
beta-Ala + CO2
show the reaction diagram
-
-
-
-
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
show the reaction diagram
additional information
?
-
Q8K566
rate-limiting enzyme for biosynthesis of taurine which is essential for biological processes such as development of the brain and eye, reproduction, osmoregulation as well as the anti-inflammatory activity of leukocytes
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Cysteine sulfinate
?
show the reaction diagram
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
activates enzyme form CSAD I and CSAD II
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoate)
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alpha-Methyl-DL-cysteine sulfinate
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beta-DL-Homocysteine sulfonate
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beta-Ethylidene-DL-aspartate
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mechanism-based inhibitor
beta-Methyleneaspartate
Cu2+
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Cys
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enzyme form CSAD II is inhibited, no effect on enzyme form CSAD I
cysteic acid
cysteine
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cysteine is able to enter the active site of the enzyme, interact with the pyridoxal 5'-phosphate-lysine internal aldimine, form a cysteine-pyridoxal 5'-phosphate aldimine and undergo intramolecular nucleophilic cyclization through its sulfhydryl group, leading to irreversible inactivation. Reaction is similar for aspartate decarboxylase, glutamate decarboxylase and cysteine sulfinic acid decarboxylase
D-Cysteine sulfinate
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DL-2-amino-3-phosphonopropionate
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Hg2+
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Homocysteic acid
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iodoacetamide
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iodoacetic acid
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L-cysteine sulfinate
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inhibits decarboxylation of cysteic acid
L-cysteine sulfonate
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L-Homocysteine sulfonate
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Met
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inhibits enzyme form CSAD I and CSAD II
NEM
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-
NO
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fusion protein with beta-galactosidase
noradrenaline
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reversed by addition of 0.1 mM pyridoxal 5'-phosphate
O2
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fusion protein with beta-galactosidase
p-hydroxymercuribenzoate
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Penicillamine
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reversed by addition of 0.1 mM pyridoxal 5'-phosphate
Zn2+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Sulfhydryl reducing agents
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required, e.g. dithiothreitol, 2-mercaptoethanol, reduced glutathione
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additional information
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CSAD protein level increases during adipogenic differentiation of 3T3-L1 cells and is significantly increased when cells achieve a mature adipocyte phenotype
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11
Asp
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0.66
cysteic acid
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-
0.037 - 0.94
cysteine sulfinate
0.18 - 0.2
cysteine sulfinic acids
0.536 - 0.644
cysteine sulfonate
2.9
Glu
-
brain enzyme
0.22 - 4
L-cysteic acid
1.14 - 1.16
L-cysteine sulfinate
0.14 - 2
L-cysteine sulfinic acid
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.52 - 5.86
L-cysteine sulfinate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.84 - 5.05
L-cysteine sulfinate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2 - 0.3
NO
0.22 - 0.3
O2
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.072
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0.238
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0.772
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3.61
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presence of 5 mM cysteine, pH 7.0, temperature not specified in the publication
4.89
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pH 7.0, temperature not specified in the publication
6.7
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wild-type, 25C, pH not specified in the publication
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6
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L-cysteine sulfinic acid, brain enzyme
additional information
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6 - 8
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about 75% of maximal activity at pH 5.6 and at pH 8.0
additional information
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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CSD is expressed in the glandular epithelium of the bulbourethral gland
Manually annotated by BRENDA team
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level of enzyme mRNA and protein increases from testis to epididymis to ductus deferens, main cell types containing enzyme are Leydig cells of testis, epithelial cells and some stromal cells
Manually annotated by BRENDA team
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; level of enzyme mRNA and protein increases from testis to epididymis to ductus deferens, main cell types containing enzyme are Leydig cells of testis, epithelial cells and some stromal cells
Manually annotated by BRENDA team
of embryo
Manually annotated by BRENDA team
pronephric duct of embryo
Manually annotated by BRENDA team
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CSD is expressed in the epithelial cells of the intermediate segments of prostate gland
Manually annotated by BRENDA team
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CSD is expressed in the tall columnar cells of the seminal vesicle
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53000
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SDS-PAGE
55000
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SDS-PAGE
56000
CSD-FLAG fusion protein, SDS-PAGE
56200
calculated from sequence
63000
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gel filtration
66000
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gel filtration
70000
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nondenaturing PAGE
75000
CDO-CSD fusion protein, SDS-PAGE
79600
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gel filtration
82100
CDO-CSD fusion protein, predicted
90000
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nondenaturing PAGE
96000
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analytical ultracentrifugation
100000
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gel filtration, sucrose density gradient centrifugation, nondenaturing PAGE
105000
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nondenaturing PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 56000, SDS-PAGE, CSD-FLAG fusion protein
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
homology modeling and substrate docking suggest that residue Q377, localized at the active site of aspartate decarboxylase, can better interact with aspartate through hydrogen bonding, which may play a role in aspartate selectivity. A leucine residue in mammalian CSADC occupies the same position
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57
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thermal inactivation at
59
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thermal inactivation at
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
pyridoxal 5'-phosphate protects against denaturation by heat or urea
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pyridoxal 5'-phosphate stabilizes
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sulfhydryl reagents are necessary to maintain maximal activity throughout purification
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 30% loss of activity after 10 days, complete loss of activity after 6 weeks
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-20C, with EDTA, pyridoxal 5'-phosphate and dithiothreitol, 3-5 mg of protein, 25-30% loss of activity
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4C, 15% loss of activity after 6 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5 distinct enzyme species
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multiple isoforms
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli JM109 cells
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subcloned into an expression vector, pESC-TRP, for Saccharomyces cerevisiae
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
bile acids regulate cysteine sulfinic acid decarboxylase mRNA expression in a feedback fashion via mechanisms involving farnesoid X receptor small heterodimer partner Shp and farnesoid X receptor
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transcripts are maternally deposited
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Q377L
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mutation diminishes the decarboxylation activity to aspartate with no major effect on its activity to cysteine sulfinic acid. Mutation leads to increase in the zwitterion form of the internal aldimine tautomer
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
3.6% of patients suffering from autoimmune polyendocrine syndrome type 1 are positive for antibodies against the enzyme. Antibodies cross-react with glutamic acid decarboxylase, aromatic L-amino acid decarboxylase and histidine decarboxylase
nutrition
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mice supplemented with dietary cholate exhibit reduced hepatic cysteine sulfinic acid decarboxylase mRNA while those receiving cholestyramine exhibit increased mRNA. Activation of farnesoid X receptor suppresses cysteine sulfinic acid decarboxylase mRNA expression whereas cysteine sulfinic acid decarboxylase expression is increased in mice lacking farnesoid X receptor small heterodimer partner Shp. Hepatic hypotaurine concentration, the product of cysteine sulfinic acid decarboxylase, is higher in Shp-/- mice with a corresponding increase in serum taurine conjugated bile acids. Fibroblast growth factor 19 administration suppresses hepatic cholesterol 7-alpha-hydroxylase CYP7A1 mRNA but does not change cysteine sulfinic acid decarboxylase mRNA expression