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
4.1.1.29
-
RECOMMENDED NAME
GeneOntology No.
Sulfinoalanine decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
3-sulfino-L-alanine = hypotaurine + CO2
show the reaction diagram
stereochemistry, replacement of carboxyl by solvent hydrogen proceeds with retention of configuration
-
3-sulfino-L-alanine = hypotaurine + CO2
show the reaction diagram
reaction proceeds via radical mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
-
Taurine and hypotaurine metabolism
-
taurine biosynthesis
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CAD
-
-
-
-
CADCase
-
-
-
-
CSAD
-
-
-
-
CSAD
Q5U3I6
-
CSAD
-
-
CSAD
-
-
CSAD/CAD
-
-
-
-
CSADCase
-
-
-
-
CSADI
-
-
CSADII
-
-
CSD
-
-
-
-
CSD
Q2PFL0
-
CSD
Q8K566
-
CSD
no activity in Katsuwonus pelamis, Oncorhynchus mykiss, Paralichthys olivaceus
-
-
Cysteic acid decarboxylase
-
-
-
-
Cysteic decarboxylase
-
-
-
-
Cysteine sulfinate decarboxylase
-
-
-
-
Cysteine sulfinate decarboxylase
Q2PFL0
-
Cysteine sulfinate decarboxylase
-
-
Cysteine sulfinate decarboxylase
-
-
Cysteine sulfinic acid decarboxylase
-
-
-
-
Cysteine sulfinic acid decarboxylase
-
-
Cysteine-sulfinate decarboxylase
-
-
-
-
Cysteine-sulfinate decarboxylase
-
-
Cysteinesulfinate decarboxylase
-
-
-
-
Cysteinesulfinic acid decarboxylase
-
-
-
-
Cysteinesulfinic acid decarboxylase
-
-
Decarboxylase, cysteinesulfinate
-
-
-
-
L-Cysteine sulfinate carboxy-lyase
-
-
-
-
L-Cysteinesulfinic acid decarboxylase
-
-
-
-
Sulfinoalanine decarboxylase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
62213-10-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
patients suffering from autoimmune polyendocrine syndrome type 1
Uniprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
no activity in Katsuwonus pelamis
no activity in liver and hepatopancreas
-
-
Manually annotated by BRENDA team
no activity in Seriola quinqueradiata
-
-
-
Manually annotated by BRENDA team
no activity in Thunnus thynnus
no activity in liver and hepatopancreas
-
-
Manually annotated by BRENDA team
strains: F344, Sprague-Dawley and F344/Brown-Norway hybrid
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
cysteine sulfinate decarboxylase is the main rate-limiting enzyme for taurine synthesis
physiological function
-, Q5U3I6
knockdown of expression significantly reduces the embryonic taurine level, and the affected embryos have increased early mortality and cardiac anomalies
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-sulfino-L-alanine
hypotaurine + CO2
show the reaction diagram
-, Q2PFL0
-
-
-
?
Cysteic acid
2-Aminoethane sulfonate + CO2
show the reaction diagram
-
-
-
-
-
Cysteic acid
2-Aminoethane sulfonate + CO2
show the reaction diagram
-
-
-
-
-
Cysteic acid
2-Aminoethane sulfonate + CO2
show the reaction diagram
-
-
-
-
?
Cysteic acid
2-Aminoethane sulfonate + CO2
show the reaction diagram
-
-
-
-
-
Cysteine sulfinate
?
show the reaction diagram
-
main enzyme of the biosynthetic pathway from Cys via cysteine sulfinate and hypotaurine to taurine
-
-
-
Cysteine sulfinate
?
show the reaction diagram
-
repressed by the action of the steroid family hormones triiodothyronine and estrogen
-
-
-
Cysteine sulfinate
?
show the reaction diagram
-
activity may be specifically regulated by sulfur amino acids metabolized by the S-adenosylmethionine-dependent pathway of methionine metabolism
-
-
-
Cysteine sulfinate
?
show the reaction diagram
-
overexpression of the enzyme stimulated by hepatocarcinogenesis results in autoantibody production
-
-
-
Cysteine sulfinate
?
show the reaction diagram
-
enzyme is responsible for biosynthesis of taurine
-
-
-
Cysteine sulfinate
?
show the reaction diagram
-
enzyme is responsible for biosynthesis of taurine
-
-
-
Cysteine sulfinate
?
show the reaction diagram
-
the enzyme initiates a pathway leading to taurine
-
-
-
Cysteine sulfinate
?
show the reaction diagram
-
thyroid hormone status modulates the activity of the enzyme
-
-
-
Cysteine sulfonate
?
show the reaction diagram
-
-
-
-
-
Cysteine sulfonate
?
show the reaction diagram
-
at 8.0% of the activity with L-cysteine sulfinate
-
-
-
Glu
4-Aminobutanoate + CO2
show the reaction diagram
-
-
-
-
-
Glu
4-Aminobutanoate + CO2
show the reaction diagram
-
L-Glu is not decarboxylated
-
-
-
Glu
4-Aminobutanoate + CO2
show the reaction diagram
-
L-Glu is not decarboxylated
-
-
-
Glu
4-Aminobutanoate + CO2
show the reaction diagram
-
very slowly
-
-
L-Asp
beta-Ala + CO2
show the reaction diagram
-
-
-
-
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
show the reaction diagram
-
-
-
-
-
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
show the reaction diagram
-
-
-
-
?
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
show the reaction diagram
-
-
-
-
?
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
show the reaction diagram
-
-
-
-
-
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
show the reaction diagram
-
-
-
-
?
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
show the reaction diagram
-
-
-
-
-
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
show the reaction diagram
-
-
-
-
-
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
show the reaction diagram
-
-
i.e. hypotaurine
-
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
show the reaction diagram
-
no activity with D-cysteine sulfinate
-
-
-
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
show the reaction diagram
-
besides its activity to aspartate, the mosquito enzyme catalyzes the decarboxylation of cysteine sulfinic acid and cysteic acid as efficiently as those of mammalian CSADC under the same testing conditions
-
-
?
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Cysteine sulfinate
?
show the reaction diagram
-
main enzyme of the biosynthetic pathway from Cys via cysteine sulfinate and hypotaurine to taurine
-
-
-
Cysteine sulfinate
?
show the reaction diagram
-
repressed by the action of the steroid family hormones triiodothyronine and estrogen
-
-
-
Cysteine sulfinate
?
show the reaction diagram
-
activity may be specifically regulated by sulfur amino acids metabolized by the S-adenosylmethionine-dependent pathway of methionine metabolism
-
-
-
Cysteine sulfinate
?
show the reaction diagram
-
overexpression of the enzyme stimulated by hepatocarcinogenesis results in autoantibody production
-
-
-
Cysteine sulfinate
?
show the reaction diagram
-
enzyme is responsible for biosynthesis of taurine
-
-
-
Cysteine sulfinate
?
show the reaction diagram
-
enzyme is responsible for biosynthesis of taurine
-
-
-
Cysteine sulfinate
?
show the reaction diagram
-
the enzyme initiates a pathway leading to taurine
-
-
-
Cysteine sulfinate
?
show the reaction diagram
-
thyroid hormone status modulates the activity of the enzyme
-
-
-
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
show the reaction diagram
-
-
-
-
?
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
coenzyme
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mn2+
-
activates enzyme form CSAD I and CSAD II
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoate)
-
-
alpha-Methyl-DL-cysteine sulfinate
-
-
beta-DL-Homocysteine sulfonate
-
-
beta-Ethylidene-DL-aspartate
-
mechanism-based inhibitor
beta-Methyleneaspartate
-
potent irreversible
beta-Methyleneaspartate
-
mechanism-based
Cys
-
enzyme form CSAD II is inhibited, no effect on enzyme form CSAD I
cysteic acid
-
inhibits decarboxylation of cysteine sulfinic acid
cysteic acid
-
-
cysteic acid
-
-
cysteic acid
-
enzyme form CSAD II is inhibited, no effect on enzyme form CSAD I
cysteine
-
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
-
-
DL-2-amino-3-phosphonopropionate
-
-
Glu
-
brain enzyme
Glu
-
competitive with cysteic acid
Homocysteic acid
-
-
iodoacetamide
-
-
iodoacetic acid
-
-
L-cysteine sulfinate
-
inhibits decarboxylation of cysteic acid
L-cysteine sulfonate
-
-
L-Homocysteine sulfonate
-
-
Met
-
inhibits enzyme form CSAD I and CSAD II
NO
-
fusion protein with beta-galactosidase
noradrenaline
-
reversed by addition of 0.1 mM pyridoxal 5'-phosphate
O2
-
fusion protein with beta-galactosidase
p-hydroxymercuribenzoate
-
-
Penicillamine
-
reversed by addition of 0.1 mM pyridoxal 5'-phosphate
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Sulfhydryl reducing agents
-
required, e.g. dithiothreitol, 2-mercaptoethanol, reduced glutathione
-
additional information
-
CSAD protein level increases during adipogenic differentiation of 3T3-L1 cells and is significantly increased when cells achieve a mature adipocyte phenotype
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.66
-
cysteic acid
-
-
0.037
-
cysteine sulfinate
-
-
0.11
-
cysteine sulfinate
-
minor enzyme form
0.121
-
cysteine sulfinate
-
major enzyme form
0.17
-
cysteine sulfinate
-
-
0.94
-
cysteine sulfinate
-
-
0.18
-
cysteine sulfinic acids
-
-
-
0.2
-
cysteine sulfinic acids
-
-
-
0.536
-
cysteine sulfonate
-
minor enzyme form
0.644
-
cysteine sulfonate
-
major enzyme form
2.9
-
Glu
-
brain enzyme
0.22
-
L-cysteic acid
-
-
0.4
-
L-cysteic acid
-
liver enzyme
4
-
L-cysteic acid
-
brain enzyme
1.14
-
L-cysteine sulfinate
-
mutant Q37L, 25C, pH not specified in the publication
1.16
-
L-cysteine sulfinate
-
wild-type, 25C, pH not specified in the publication
0.14
-
L-cysteine sulfinic acid
-
liver enzyme
2
-
L-cysteine sulfinic acid
-
brain enzyme
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5.52
-
L-cysteine sulfinate
-
mutant Q377L, 25C, pH not specified in the publication
5.86
-
L-cysteine sulfinate
-
wild-type, 25C, pH not specified in the publication
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4.84
-
L-cysteine sulfinate
-
mutant Q37L, 25C, pH not specified in the publication
5564
5.05
-
L-cysteine sulfinate
-
wild-type, 25C, pH not specified in the publication
5564
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.2
-
NO
-
CSADII fusion protein with beta-galactosidase
0.3
-
NO
-
CSADI fusion protein with beta-galactosidase
0.22
-
O2
-
CSADII fusion protein with beta-galactosidase
0.3
-
O2
-
CSADI fusion protein with beta-galactosidase
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.072
-
-
-
0.21
-
-
-
0.238
-
-
-
0.772
-
-
-
1.67
-
-
-
3.61
-
-
presence of 5 mM cysteine, pH 7.0, temperature not specified in the publication
4.89
-
-
pH 7.0, temperature not specified in the publication
6.7
-
-
wild-type, 25C, pH not specified in the publication
additional information
-
-
-
additional information
-
-
HPLC method for assaying is applicable to study the dietary regulation of cysteinesulfinic acid decarboxylase in rat tissues
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
-
L-cysteine sulfinic acid, cysteic acid
7
-
-
enzyme form CSAD II
7.2
-
-
-
7.2
-
-
enzyme form CSAD I
7.4
-
-
L-cysteine sulfinic acid, cysteic acid, liver enzyme
7.4
-
-
L-cysteic acid
7.6
-
-
L-cysteine sulfinic acid, brain enzyme
additional information
-
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.6
8
-
about 75% of maximal activity at pH 5.6 and at pH 8.0
additional information
-
-
-
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
cerebellum
Manually annotated by BRENDA team
-
cerebellum, medulla oblongata, pons, hypothalamus, striatum, midbrain, hippocampus, cerebral cortex
Manually annotated by BRENDA team
-
immunocytochemical visualization of sulfinoalanine decarboxylase with a specific antiserum
Manually annotated by BRENDA team
-
glial localization in cerebellum
Manually annotated by BRENDA team
-
strictly localized in astrocytes in the cerebellum and in the hippocampus
Manually annotated by BRENDA team
-
astrocytes in the cerebellum and hippocampus
Manually annotated by BRENDA team
-, Q5U3I6
of embryo
Manually annotated by BRENDA team
-
CSD is expressed in the glandular epithelium of the bulbourethral gland
Manually annotated by BRENDA team
-
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
-
-, 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
-
restricted localization of CSD mRNA in the cortical and medullary proximal straight tubules
Manually annotated by BRENDA team
-
taurine depletion significantly elevates both hepatic and renal CSAD activity above the values for cats having normal taurine status
Manually annotated by BRENDA team
-
female livers contain only 5% of the cysteinesulfinate decarboxylase activity of male livers
Manually annotated by BRENDA team
-, Q5U3I6
of embryo
Manually annotated by BRENDA team
-
activity is almost constant throughout the fish growth cycle, CDS does not seem to be responsible for low production of taurine in juvenile fish
Manually annotated by BRENDA team
-
enzyme activity is sifgnificantly lower in aged F344 rats but not in Sprague-Dawley and F344/Brown-Norway hybrid
Manually annotated by BRENDA team
-
taurine depletion significantly elevates both hepatic and renal CSAD activity above the values for cats having normal taurine status
Manually annotated by BRENDA team
-, Q5U3I6
of embryo
Manually annotated by BRENDA team
-, Q5U3I6
of embryo
Manually annotated by BRENDA team
-, Q5U3I6
pronephric duct of embryo
Manually annotated by BRENDA team
-
CSD is expressed in the epithelial cells of the intermediate segments of prostate gland
Manually annotated by BRENDA team
-
concentrated in the inner plexiform layer, in the amacrine cells
Manually annotated by BRENDA team
-, Q5U3I6
of embryo
Manually annotated by BRENDA team
-
CSD is expressed in the tall columnar cells of the seminal vesicle
Manually annotated by BRENDA team
-
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
additional information
-
tissue specificity
Manually annotated by BRENDA team
additional information
-, Q5U3I6
enzyme is expressed in yolk syncytial layer and various embryonic tissues such as notochord, brain, retina, pronephric duct, liver, and pancreas
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
53000
-
-
SDS-PAGE
55000
-
-
SDS-PAGE
56000
-
-, Q2PFL0
CSD-FLAG fusion protein, SDS-PAGE
56200
-
-, Q2PFL0
calculated from sequence
63000
-
-
gel filtration
66000
-
-
gel filtration
70000
-
-
nondenaturing PAGE
75000
-
-, Q2PFL0
CDO-CSD fusion protein, SDS-PAGE
79600
-
-
gel filtration
82100
-
-, Q2PFL0
CDO-CSD fusion protein, predicted
90000
-
-
nondenaturing PAGE
96000
-
-
analytical ultracentrifugation
100000
-
-
gel filtration, sucrose density gradient centrifugation, nondenaturing PAGE
105000
-
-
nondenaturing PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-, Q2PFL0
x * 56000, SDS-PAGE, CSD-FLAG fusion protein
dimer
-
2 * 55000, SDS-PAGE
dimer
-
2 * 53000, SDS-PAGE
dimer
-
2 * 43000, SDS-PAGE
monomer
-
1 * 70000, SDS-PAGE
monomer
-
1 * 51000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
57
-
-
thermal inactivation at
59
-
-
thermal inactivation at
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
pyridoxal 5'-phosphate protects against denaturation by heat or urea
-
pyridoxal 5'-phosphate stabilizes
-
sulfhydryl reagents are necessary to maintain maximal activity throughout purification
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, with EDTA, pyridoxal 5'-phosphate and dithiothreitol, 3-5 mg of protein, 25-30% loss of activity
-
-20C, 30% loss of activity after 10 days, complete loss of activity after 6 weeks
-
4C, 15% loss of activity after 6 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
5 distinct enzyme species
-
multiple isoforms
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
subcloned into an expression vector, pESC-TRP, for Saccharomyces cerevisiae
-, Q2PFL0
-
Q8K566
expressed in Escherichia coli JM109 cells
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
transcripts are maternally deposited
-, Q5U3I6
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
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Q377L
-
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
-, G8FGR5
the dominant melanic mutation called chocolate implicates the gene encoding pyridoxal phosphate-dependant cysteine sulfinic acid decarboxylase. Mutation causes a dramatic darkening of larvae, without having any detectable effects during other developmental stages
additional information
-, Q2PFL0
CDO-CSD fusion protein, cysteine dioxygenase and cysteine sulfinate decarboxylase
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
Q9Y600
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