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Information on EC 4.1.1.29 - sulfinoalanine decarboxylase
for references in articles please use BRENDA:EC4.1.1.29
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EC Tree 4 Lyases
4.1 Carbon-carbon lyases
4.1.1 Carboxy-lyases
4.1.1.29 sulfinoalanine decarboxylase
IUBMB Comments
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.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 4.1.1.29
- dioxygenase
-
taut
- cystathionase
-
transsulfuration
-
taurine-deficient
-
taurine-free
- nutrition
- medicine
showSynonyms
cysteine sulfinic acid decarboxylase, cysteine sulfinate decarboxylase, cysteinesulfinate decarboxylase, cysteinesulfinic acid decarboxylase, cysteine-sulfinate decarboxylase, cgcsad1, undec1a, cgcsad2, l-cysteine sulfinate decarboxylase, csadcase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CAD
-
-
-
-
CADCase
-
-
-
-
CSAD
CSAD/CAD
-
-
-
-
CSADCase
-
-
-
-
CSD
Cysteic acid decarboxylase
-
-
-
-
Cysteic decarboxylase
-
-
-
-
Cysteine sulfinate decarboxylase
Cysteine sulfinic acid decarboxylase
Cysteine-sulfinate decarboxylase
Cysteinesulfinate decarboxylase
-
-
-
-
Cysteinesulfinic acid decarboxylase
Decarboxylase, cysteinesulfinate
-
-
-
-
L-Cysteine sulfinate carboxy-lyase
-
-
-
-
L-Cysteinesulfinic acid decarboxylase
-
-
-
-
Sulfinoalanine decarboxylase
-
-
-
-
CSAD
-
-
-
-
CSD
-
-
-
-
Cysteine sulfinate decarboxylase
-
-
-
-
Cysteine sulfinic acid decarboxylase
-
-
-
-
Cysteine-sulfinate decarboxylase
-
-
-
-
Cysteinesulfinic acid decarboxylase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-sulfino-L-alanine = hypotaurine + CO2
stereochemistry, replacement of carboxyl by solvent hydrogen proceeds with retention of configuration
-
3-sulfino-L-alanine = hypotaurine + CO2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
taurine biosynthesis I
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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.
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CAS REGISTRY NUMBER
COMMENTARY
62213-10-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cysteine sulfinic acid
hypotaurine + CO2
Substrates: -
Products: -
Products: -
?
L-aspartate
beta-alanine + CO2
Substrates: reaction of EC 4.1.1.11
Products: -
Products: -
?
3-sulfino-L-alanine
hypotaurine + CO2
Substrates: -
Products: -
Products: -
?
3-sulfino-L-alanine
hypotaurine + CO2
Substrates: -
Products: -
Products: -
?
3-sulfino-L-alanine
hypotaurine + CO2
Substrates: -
Products: -
Products: -
?
3-sulfino-L-alanine
hypotaurine + CO2
Substrates: -
Products: -
Products: -
?
3-sulfino-L-alanine
hypotaurine + CO2
Substrates: -
Products: -
Products: -
?
3-sulfino-L-alanine
hypotaurine + CO2
Substrates: -
Products: -
Products: -
?
3-sulfino-L-alanine
hypotaurine + CO2
Substrates: -
Products: -
Products: -
?
3-sulfino-L-alanine
hypotaurine + CO2
Substrates: -
Products: -
Products: -
?
Cysteic acid
2-Aminoethane sulfonate + CO2
-
Substrates: -
Products: -
Products: -
?
Cysteine sulfinate
?
-
Substrates: enzyme is responsible for biosynthesis of taurine
Products: -
Products: -
?
Cysteine sulfinate
?
-
Substrates: main enzyme of the biosynthetic pathway from Cys via cysteine sulfinate and hypotaurine to taurine
Products: -
Products: -
?
Cysteine sulfinate
?
-
Substrates: repressed by the action of the steroid family hormones triiodothyronine and estrogen
Products: -
Products: -
?
Cysteine sulfinate
?
-
Substrates: activity may be specifically regulated by sulfur amino acids metabolized by the S-adenosylmethionine-dependent pathway of methionine metabolism
Products: -
Products: -
?
Cysteine sulfinate
?
-
Substrates: overexpression of the enzyme stimulated by hepatocarcinogenesis results in autoantibody production
Products: -
Products: -
?
Cysteine sulfinate
?
-
Substrates: enzyme is responsible for biosynthesis of taurine
Products: -
Products: -
?
Cysteine sulfinate
?
-
Substrates: the enzyme initiates a pathway leading to taurine
Products: -
Products: -
?
Cysteine sulfinate
?
-
Substrates: thyroid hormone status modulates the activity of the enzyme
Products: -
Products: -
?
Cysteine sulfonate
?
-
Substrates: at 8.0% of the activity with L-cysteine sulfinate
Products: -
Products: -
?
Glu
4-Aminobutanoate + CO2
-
Substrates: L-Glu is not decarboxylated
Products: -
Products: -
?
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
-
Substrates: 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
Products: -
Products: -
?
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
-
Substrates: -
Products: -
Products: -
?
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
-
Substrates: -
Products: -
Products: -
?
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
-
Substrates: -
Products: -
Products: -
?
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
-
Substrates: -
Products: i.e. hypotaurine
Products: i.e. hypotaurine
?
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
-
Substrates: -
Products: -
Products: -
?
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
-
Substrates: no activity with D-cysteine sulfinate
Products: -
Products: -
?
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
-
Substrates: -
Products: -
Products: -
?
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Q8K566
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: no decarboxylation activity toward cysteic acid and glutamate
Products: -
Products: -
-
additional information
?
-
Substrates: substrate specificity, overview. Substrate analogues L-cysteine, L-proline, L-alanine, L-glutamate, and L-asparagxadinate (at 5 mM) are also used as substrates by enzyme mutant Undec1A-1180, highest activity with L-cysteine, low activity with L-proline, no activity with L-alanine
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-sulfino-L-alanine
hypotaurine + CO2
Substrates: -
Products: -
Products: -
?
3-sulfino-L-alanine
hypotaurine + CO2
Substrates: -
Products: -
Products: -
?
3-sulfino-L-alanine
hypotaurine + CO2
Substrates: -
Products: -
Products: -
?
3-sulfino-L-alanine
hypotaurine + CO2
Substrates: -
Products: -
Products: -
?
3-sulfino-L-alanine
hypotaurine + CO2
Substrates: -
Products: -
Products: -
?
3-sulfino-L-alanine
hypotaurine + CO2
Substrates: -
Products: -
Products: -
?
3-sulfino-L-alanine
hypotaurine + CO2
Substrates: -
Products: -
Products: -
?
Cysteine sulfinate
?
-
Substrates: enzyme is responsible for biosynthesis of taurine
Products: -
Products: -
?
Cysteine sulfinate
?
-
Substrates: main enzyme of the biosynthetic pathway from Cys via cysteine sulfinate and hypotaurine to taurine
Products: -
Products: -
?
Cysteine sulfinate
?
-
Substrates: repressed by the action of the steroid family hormones triiodothyronine and estrogen
Products: -
Products: -
?
Cysteine sulfinate
?
-
Substrates: activity may be specifically regulated by sulfur amino acids metabolized by the S-adenosylmethionine-dependent pathway of methionine metabolism
Products: -
Products: -
?
Cysteine sulfinate
?
-
Substrates: overexpression of the enzyme stimulated by hepatocarcinogenesis results in autoantibody production
Products: -
Products: -
?
Cysteine sulfinate
?
-
Substrates: enzyme is responsible for biosynthesis of taurine
Products: -
Products: -
?
Cysteine sulfinate
?
-
Substrates: the enzyme initiates a pathway leading to taurine
Products: -
Products: -
?
Cysteine sulfinate
?
-
Substrates: thyroid hormone status modulates the activity of the enzyme
Products: -
Products: -
?
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
-
Substrates: -
Products: -
Products: -
?
L-Cysteine sulfinate
2-Aminoethane sulfinate + CO2
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
two PLP molecules are located in the active site at the interface between two monomers
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
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
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Autoimmune Diseases
Analysis of antibody reactivity against cysteine sulfinic acid decarboxylase, a pyridoxal phosphate-dependent enzyme, in endocrine autoimmune disease.
Cardiomegaly
Dysfunction of myocardial taurine transport and effect of taurine supplement in rats with isoproterenol-induced myocardial injury.
Melanosis
Genetic basis of stage-specific melanism: a putative role for a cysteine sulfinic acid decarboxylase in insect pigmentation.
Seizures
Oxygen-induced seizures and inhibition of human glutamate decarboxylase and porcine cysteine sulfinic acid decarboxylase by oxygen and nitric oxide.
Vitamin B 6 Deficiency
Cysteine sulfinic acid decarboxylase in rat brain: effect of vitamin B6 deficiency on soluble and particulate components.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.1
3-sulfino-L-alanine
pH 7.0, 35°C, recombinant mutant V81L/F240S/I250S/D266L enzyme
1.56
3-sulfino-L-alanine
pH 7.0, 35°C, recombinant wild-type enzyme
1.14
L-cysteine sulfinate
-
mutant Q37L, 25°C, pH not specified in the publication
1.16
L-cysteine sulfinate
-
wild-type, 25°C, pH not specified in the publication
additional information
additional information
Lineweaver-Burk plots
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.763
3-sulfino-L-alanine
pH 7.0, 35°C, recombinant wild-type enzyme
1.476
3-sulfino-L-alanine
pH 7.0, 35°C, recombinant mutant V81L/F240S/I250S/D266L enzyme
5.52
L-cysteine sulfinate
-
mutant Q377L, 25°C, pH not specified in the publication
5.86
L-cysteine sulfinate
-
wild-type, 25°C, pH not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.49
3-sulfino-L-alanine
pH 7.0, 35°C, recombinant wild-type enz.yme
1.34
3-sulfino-L-alanine
pH 7.0, 35°C, recombinant mutant V81L/F240S/I250S/D266L enzyme
4.84
L-cysteine sulfinate
-
mutant Q37L, 25°C, pH not specified in the publication
5.05
L-cysteine sulfinate
-
wild-type, 25°C, pH not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.61
-
presence of 5 mM cysteine, pH 7.0, temperature 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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
7.4
7
recombinant His-tagged wild-type and mutant enzymes
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
recombinant His-tagged wild-type and mutant enzymes
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
obtained at hydrothermal vent field in Myojin Knoll (depth, 1228 m), Japan
UniProt
brenda
patients suffering from autoimmune polyendocrine syndrome type 1
Uniprot
brenda
CSAD1; has two copies of cysteine sulfinate decarboxylase (CSAD), CgCSAD1 and CgCSAD2, from two different wild populations Weihai (salinity 30) and Dongying (salinity 16) in 2015
UniProt
brenda
CSAD2; has two copies of cysteine sulfinate decarboxylase (CSAD), CgCSAD1 and CgCSAD2, from two different wild populations Weihai (salinity 30) and Dongying (salinity 16) in 2015
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
CSD is expressed in the glandular epithelium of the bulbourethral gland
brenda
-
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
brenda
-
CSD is expressed in the epithelial cells of the intermediate segments of prostate gland
brenda
CSD messenger RNA (mRNA) and protein are expressed in the major salivary glands of male mice. The relative levels of CSD mRNA increase from the submandibular gland (SMG) to the sublingual gland (SLG) and parotid gland (PG), but the levels of the CSD protein are the opposite
brenda
-
CSD is expressed in the tall columnar cells of the seminal vesicle
brenda
additional information
-
cerebellum, medulla oblongata, pons, hypothalamus, striatum, midbrain, hippocampus, cerebral cortex
brenda
-
immunocytochemical visualization of sulfinoalanine decarboxylase with a specific antiserum
brenda
-
strictly localized in astrocytes in the cerebellum and in the hippocampus
brenda
-
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
brenda
isozyme CSAD1 shows highest expression levels in gonads and hemolymph
brenda
isozyme CSAD2 shows highest expression levels in gonads and hemolymph
brenda
isozyme CSAD1 shows highest expression levels in gonads and hemolymph
brenda
isozyme CSAD2 shows highest expression levels in gonads and hemolymph
brenda
-
taurine depletion significantly elevates both hepatic and renal CSAD activity above the values for cats having normal taurine status
brenda
-
restricted localization of CSD mRNA in the cortical and medullary proximal straight tubules
brenda
-
taurine depletion significantly elevates both hepatic and renal CSAD activity above the values for cats having normal taurine status
brenda
-
activity is almost constant throughout the fish growth cycle, CDS does not seem to be responsible for low production of taurine in juvenile fish
brenda
-
female livers contain only 5% of the cysteinesulfinate decarboxylase activity of male livers
brenda
-
enzyme activity is sifgnificantly lower in aged F344 rats but not in Sprague-Dawley and F344/Brown-Norway hybrid
brenda
-
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
brenda
additional information
tissue-specific expression pattern of CSAD isozymes, overview. The enzyme is ubiquitously expressed with highest level of enzyme in gills
brenda
additional information
-
tissue-specific expression pattern of CSAD isozymes, overview. The enzyme is ubiquitously expressed with highest level of enzyme in gills
brenda
additional information
enzyme is expressed in yolk syncytial layer and various embryonic tissues such as notochord, brain, retina, pronephric duct, liver, and pancreas
brenda
additional information
-
enzyme is expressed in yolk syncytial layer and various embryonic tissues such as notochord, brain, retina, pronephric duct, liver, and pancreas
brenda
additional information
tissue-specific expression pattern of CSAD isozymes, overview. Expression levels of isozyme CSAD1 are higher compared to isozyme CSAD2
brenda
additional information
tissue-specific expression pattern of CSAD isozymes, overview. Expression levels of isozyme CSAD1 are higher compared to isozyme CSAD2
brenda
additional information
the enzyme is mainly located in the excretory ducts (EDs) and interlobular duct (IL) of submandibular gland (SMG) and ED in sublingual gland (SLG), respectively. The relative levels of CSD mRNA increase from the submandibular gland (SMG) to the sublingual gland (SLG) and parotid gland (PG), but the levels of the CSD protein are the opposite. Immunofluorescence for the expression of CSD and alpha-SMA in SMG, SLG, and PG
brenda
additional information
no enzyme expression in skeletal muscle
brenda
additional information
no enzyme expression in gill, heart, stomach, pancreas, and skeletal and dark muscles
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
the CSAD1 sequence contains no signal peptide
-
brenda
additional information
the CSAD1 sequence contains no signal peptide
-
brenda
additional information
the CSAD2 sequence contains no signal peptide
-
brenda
additional information
the CSAD2 sequence contains no signal peptide
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
CSAD is a member of the type II PLP-dependent amino acid decarboxylase carboxylase family
malfunction
the mutant Undec1A-1180 has 5.62fold highxader specific activity than wild-type Undec1A
metabolism
CSAD gene is the key enzyme in the pathway of taurine biosynthesis
physiological function
additional information
structure homology modelling and molecular docking, overview
physiological function
-
cysteine sulfinate decarboxylase is the main rate-limiting enzyme for taurine synthesis
physiological function
knockdown of expression significantly reduces the embryonic taurine level, and the affected embryos have increased early mortality and cardiac anomalies
physiological function
cysteine sulfinic acid decarboxylase catalyzes the reaction of decarboxylation of cysteine sulfinic acid into hypotaurine. This step is considered as a rate-limiting step of taurine biosynthesis. Marine fish generally show low taurine synthesis activity
physiological function
cysteine sulfinic acid decarboxylase catalyzes the reaction of decarboxylation of cysteine sulfinic acid into hypotaurine. This step is considered as a rate-limiting step of taurine biosynthesis. Marine fish generally show low taurine synthesis activity
physiological function
cysteine sulfinic acid decarboxylase catalyzes the reaction of decarboxylation of cysteine sulfinic acid into hypotaurine. This step is considered as a rate-limiting step of taurine biosynthesis. Marine fish generally show low taurine synthesis activity
physiological function
cysteine sulfinic acid decarboxylase catalyzes the reaction of decarboxylation of cysteine sulfinic acid into hypotaurine. This step is considered as a rate-limiting step of taurine biosynthesis. Marine fish generally show low taurine synthesis activity
physiological function
cysteine sulfinic acid decarboxylase catalyzes the reaction of decarboxylation of cysteine sulfinic acid into hypotaurine. This step is considered as a rate-limiting step of taurine biosynthesis. Marine fish generally show low taurine synthesis activity
physiological function
-
cysteine sulfinic acid decarboxylase catalyzes the reaction of decarboxylation of cysteine sulfinic acid into hypotaurine. This step is considered as a rate-limiting step of taurine biosynthesis. Marine fish generally show low taurine synthesis activity
physiological function
-
cysteine sulfinic acid decarboxylase catalyzes the reaction of decarboxylation of cysteine sulfinic acid into hypotaurine. This step is considered as a rate-limiting step of taurine biosynthesis. Marine fish generally show low taurine synthesis activity
physiological function
-
cysteine sulfinic acid decarboxylase catalyzes the reaction of decarboxylation of cysteine sulfinic acid into hypotaurine. This step is considered as a rate-limiting step of taurine biosynthesis. Marine fish generally show low taurine synthesis activity
physiological function
CSAD gene is the key enzyme in the pathway of taurine biosynthesis
physiological function
the gills of Bathymodiolus septemdierum maintain high levels of expression of the CSAD gene regardless of ambient sulfide level and accumulate hypotaurine continuously to protect against sudden exposure to high level of sulfide. Since CSAD gene expression is observed in all the tissues examined, it is likely that hypotaurine is synthesized extensively in mussel tissues
physiological function
CSD is the rate-limiting enzyme of taurine biosynthesis
physiological function
CSD is the rate-limiting enzyme of taurine biosynthesis
physiological function
cysteine sulfinic acid decarboxylase catalyzes the reaction of decarboxylation of cysteine sulfinic acid into hypotaurine. This step is considered as a rate-limiting step of taurine biosynthesis. Marine fish generally show low taurine synthesis activity
physiological function
cysteine sulfinic acid decarboxylase catalyzes the reaction of decarboxylation of cysteine sulfinic acid into hypotaurine. This step is considered as a rate-limiting step of taurine biosynthesis. Marine fish generally show low taurine synthesis activity
physiological function
cysteine sulfinic acid decarboxylase catalyzes the reaction of decarboxylation of cysteine sulfinic acid into hypotaurine. This step is considered as a rate-limiting step of taurine biosynthesis. Marine fish generally show low taurine synthesis activity
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A0N9E6Z6_PAGMA
508
0
57342
TrEMBL
Secretory Pathway (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
-
gel filtration, sucrose density gradient centrifugation, nondenaturing PAGE
53000
55000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
dimer
2 * 66400, SDS-PAGE, 2 * 61152, calculated from sequence, recombinant His-tagged protein
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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
-
structure of GADL1, together with a solution model based on small-angle X-ray scattering data. GADL1 adopts a more loose conformation in solution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
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
G369A
mutant shows both improved thermostability and higher activity
V81L/F240S/I250S/D266L
generation of mutant Undec1A-1180 by random mutagenxadesis through sequential error-prone PCR from a mutagenesis library. The mutant has 5.62fold highxader specific activity than wild-type Undec1A at 35°C and pH 7.0. The optimum pH of Undec1A-1180 does not change. Molecular docking results indicatxade that amino acid residues Ala235, Val237, Asp239, Ile267, Ala268, and Lys298 in mutant Unxaddec1A-1180 protein help recognize substrate molecules and catalyze the reaction with of L-cysteine sulfinic acid. Mutation efficiency analysis of different combinations of Mg2+ and Mn2+, overview
additional information
additional information
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
-
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
CDO-CSD fusion protein, cysteine dioxygenase and cysteine sulfinate decarboxylase
additional information
-
CDO-CSD fusion protein, cysteine dioxygenase and cysteine sulfinate decarboxylase
additional information
generation of CSAD knockout mice, chimeric CSAD KO mice are produced by injection of cells from a gene trap ES cell line (XP0392) into C57BL/6 (B6) blastocysts which are implanted into a pseudopregnant B6 mouse. Nine chimeric mice are mated with B6 in the animal colony. Agouti mice produced by this mating are back-crossed to B6 and offsprings are genotyped using PCR, overview. Although CSAD-/- generation (G)1 and G2 survive, offspring from G2 CSAD-/- have low brain and liver taurine concentrations and most die within 24 hrs of birth. Taurine concentrations in G3 CSAD-/- born from G2 CSAD-/- treated with taurine in the drinking water are restored and survival rates of G3 CSAD-/- increase from 15% to 92%. The mRNA expression of CDO, ADO, and TauT is not different in CSAD-/- compared to wild-type, and CSAD mRNA is not expressed in CSAD-/-. Expression of Gpx 1 and 3 is increased significantly in CSAD-/- and restored to normal levels with taurine supplementation. Lactoferrin and the prolactin receptor are significantly decreased in CSAD-/-. The prolactin receptor is restored with taurine supplementation
additional information
-
generation of CSAD knockout mice, chimeric CSAD KO mice are produced by injection of cells from a gene trap ES cell line (XP0392) into C57BL/6 (B6) blastocysts which are implanted into a pseudopregnant B6 mouse. Nine chimeric mice are mated with B6 in the animal colony. Agouti mice produced by this mating are back-crossed to B6 and offsprings are genotyped using PCR, overview. Although CSAD-/- generation (G)1 and G2 survive, offspring from G2 CSAD-/- have low brain and liver taurine concentrations and most die within 24 hrs of birth. Taurine concentrations in G3 CSAD-/- born from G2 CSAD-/- treated with taurine in the drinking water are restored and survival rates of G3 CSAD-/- increase from 15% to 92%. The mRNA expression of CDO, ADO, and TauT is not different in CSAD-/- compared to wild-type, and CSAD mRNA is not expressed in CSAD-/-. Expression of Gpx 1 and 3 is increased significantly in CSAD-/- and restored to normal levels with taurine supplementation. Lactoferrin and the prolactin receptor are significantly decreased in CSAD-/-. The prolactin receptor is restored with taurine supplementation
additional information
-
generation of CSAD knockout mice, chimeric CSAD KO mice are produced by injection of cells from a gene trap ES cell line (XP0392) into C57BL/6 (B6) blastocysts which are implanted into a pseudopregnant B6 mouse. Nine chimeric mice are mated with B6 in the animal colony. Agouti mice produced by this mating are back-crossed to B6 and offsprings are genotyped using PCR, overview. Although CSAD-/- generation (G)1 and G2 survive, offspring from G2 CSAD-/- have low brain and liver taurine concentrations and most die within 24 hrs of birth. Taurine concentrations in G3 CSAD-/- born from G2 CSAD-/- treated with taurine in the drinking water are restored and survival rates of G3 CSAD-/- increase from 15% to 92%. The mRNA expression of CDO, ADO, and TauT is not different in CSAD-/- compared to wild-type, and CSAD mRNA is not expressed in CSAD-/-. Expression of Gpx 1 and 3 is increased significantly in CSAD-/- and restored to normal levels with taurine supplementation. Lactoferrin and the prolactin receptor are significantly decreased in CSAD-/-. The prolactin receptor is restored with taurine supplementation
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
30 min, 70% residual activity for wild-type, 82% for mutant G369A
50
30 min, 22% residual activity for wild-type, 39% for mutant G369A
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
sulfhydryl reagents are necessary to maintain maximal activity throughout purification
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 30% loss of activity after 10 days, complete loss of activity after 6 weeks
-
-20°C, with EDTA, pyridoxal 5'-phosphate and dithiothreitol, 3-5 mg of protein, 25-30% loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, semiquantitative real-time PCR enzyme expression analysis
gene CSAD, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR enzyme expression analysis
gene CSAD1, Crassostrea gigas has two copies of CSAD, CgCSAD1 and CgCSAD2, DNA and amino acid sequence determination and analysis, quantitative real-time PCR enzyme expression analysis
gene CSAD2, Crassostrea gigas has two copies of CSAD, CgCSAD1 and CgCSAD2, DNA and amino acid sequence determination and analysis, quantitative real-time PCR enzyme expression analysis
gene undec1A, cloned from metagenome through sequence-based screening of uncultured soil microorganisms, DNA and amino acid sequence determination and analysis, recombinant overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS
phylogenetic analysis, quantitative real-time PCR enzyme expression analysis
-
phylogenetic analysis, semiquantitative real-time PCR enzyme expression analysis
-
sequence comparisons and phylogenetic analysis, semiquantitative real-time PCR enzyme expression analysis
subcloned into an expression vector, pESC-TRP, for Saccharomyces cerevisiae
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, semiquantitative real-time PCR enzyme expression analysis
-
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, semiquantitative real-time PCR enzyme expression analysis
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, semiquantitative real-time PCR enzyme expression analysis
sequence comparisons and phylogenetic analysis, semiquantitative real-time PCR enzyme expression analysis
sequence comparisons and phylogenetic analysis, semiquantitative real-time PCR enzyme expression analysis
sequence comparisons and phylogenetic analysis, semiquantitative real-time PCR enzyme expression analysis
sequence comparisons and phylogenetic analysis, semiquantitative real-time PCR enzyme expression analysis
sequence comparisons and phylogenetic analysis, semiquantitative real-time PCR enzyme expression analysis
sequence comparisons and phylogenetic analysis, semiquantitative real-time PCR enzyme expression analysis
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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
-
the enzyme mRNA level in the gill is not significantly changed by exposure to sulfides or thiosulfate
under low salinity treatment (0.8% and 1.5%) no correlation between the expression of CSAD and different populations is observed. Isoform CgCSAD1 expression increases significantly in groups treated for 24 h
under low salinity treatment (0.8% and 1.5%) no correlation between the expression of CSAD and different populations is observed. Isoform CgCSAD2 does not show significantly altered expression
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
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
-
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
synthesis
production of beta-alanine using whole-cell catalysis was with recombinant Escherichia coli cells. One-time addition of 1 mM PLP is sufficient. The yield of beta-alanine finally reaches 836.6 mM at 21 h, with 83.7% conversion. In a fed-batch reaction, production of beta-alanine reaches nearly 100 mM, and the conversion is 90%. In a fed-batch reaction using mutant G369A, production of beta-alanine reaches nearly 1530 mM, and the conversion is 95.6%. Up to 162 g/l beta-alanine can be produced using the recombinant G369A variant
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wu, J.Y.
Purification and characterization of cysteic acid and cysteine sulfinic acid decarboxylase and L-glutamate decarboxylase from bovine brain
Proc. Natl. Acad. Sci. USA
79
4270-4274
1982
Bos taurus
brenda
Jacobsen, J.G.; Thomas, L.L.; Smith Jr., L.H.
Properties and distribution of mammalian L-cysteine sulfinate carboxy-lyase
Biochim. Biophys. Acta
85
103-116
1964
Rattus norvegicus
brenda
Guion-Rain, M.C.; Portemer, C.; Chatagner, F.
Rat liver cysteine sulfinate decarboxylase: purification, new appraisal of the molecular weight and determination of catalytic properties
Biochim. Biophys. Acta
384
265-276
1975
Rattus norvegicus
brenda
Urban, P.F.; Reichert, P.
Purification of rat brain cysteine sulphinate decarboxylase (EC 4.1.1.29)
Biochem. Soc. Trans.
9
106
1981
Rattus norvegicus
brenda
Urban, P.F.; Reichert, P.
Purification and properties of specific cysteine sulphinate decarboxylase (EC 4.1.1.29) from rat brain
Biochem. Soc. Trans.
10
59-60
1982
Rattus norvegicus
-
brenda
Griffith, O.W.
Cysteinesulfinate metabolism. Altered partitioning between transamination and decarboxylation following administration of beta-methyleneaspartate
J. Biol. Chem.
258
1591-1598
1983
Rattus norvegicus
brenda
Urban, P.F.; Reichert, P.
Immunological distribution of cysteine sulphinate decarboxylase (EC 4.1.1.29) in rat tissues
Biochem. Soc. Trans.
12
817-818
1984
Rattus norvegicus
-
brenda
Wu, J.Y.
GABA and taurine enzymes in mammalian brain
Curr. Top. Cell. Regul.
24
119-128
1984
Bos taurus, Mammalia
brenda
Weinstein, C.L.; Griffith, O.W.
Multiple forms of rat liver cysteinesulfinate decarboxylase
J. Biol. Chem.
262
7254-7263
1987
Rattus norvegicus
brenda
Aberhart, D.J.
Stereochemistry of cysteinesulphinic acid decarboxylase
J. Chem. Soc. Perkin Trans. I
1988
1547-1550
1988
Rattus norvegicus
-
brenda
Ide, T.
Simple high-performance liquid chromatographic method for assaying cysteinesulfinic acid decarboxylase activity in rat tissue
J. Chromatogr.
694
325-332
1997
Rattus norvegicus
brenda
Do, K.Q.; Tappaz, M.L.
Specificity of cysteine sulfinate decarboxylase (CSD) for sulfur-containing amino-acids
Neurochem. Int.
28
363-371
1996
Rattus norvegicus
brenda
Reymond, I.; Almarghini, K.; Tappaz, M.
Immunocytochemical localization of cysteine sulfinate decarboxylase in astrocytes in the cerebellum and hippocampus: a quantitative double immunofluorescence study with glial fibrillary acidic protein and S-100 protein
Neuroscience
75
619-633
1996
Rattus norvegicus
brenda
Jerkins, A.A.; Steele, R.D.
Cysteine sulfinic acid decarboxylase activity in response to thyroid hormone administration in rats
Arch. Biochem. Biophys.
286
428-432
1991
Rattus norvegicus
brenda
Jerkins, A.A.; Steele, R.D.
Dietary sulfur amino acid modulation of cysteine sulfinic acid decarboxylase
Am. J. Physiol.
261
E551-555
1991
Rattus norvegicus
brenda
Remy, A.; Henry, S.; Tappaz, M.
Specific antiserum and monoclonal antibodies against the taurine biosynthesis enzyme cysteine sulfinate decarboxylase: identity of brain and liver enzyme
J. Neurochem.
54
870-879
1990
Rattus norvegicus
brenda
Kaisakia, P.J.; Jerkins, A.A.; Goodspeed, D.C.; Steele, R.D.
Cloning and characterization of rat cysteine sulfinic acid decarboxylase
Biochim. Biophys. Acta
1262
79-82
1995
Rattus norvegicus
brenda
Kishimoto, T.; Kokura, K.; Nakadai, T.; Miyazawa, Y.; Wakamatsu, T.; Makino, Y.; Nakamura, T.; Hara, E.; Oda, K.; Muramatsu, M.; Tamura, T.
Overexpression of cysteine sulfinic acid decarboxylase stimulated by hepatocarcinogenesis results in autoantibody production in rats
Cancer Res.
56
5230-5237
1996
Rattus norvegicus
brenda
Almarghini, K.; Remy, A.; Tappaz, M.
Immunocytochemistry, of the taurine biosynthesis enzyme, cysteine sulfinate decarboxylase, in the cerebellum: evidence for a glial localization
Neuroscience
43
111-119
1991
Rattus norvegicus
brenda
Jin, H.; Jones, E.E.
Studies on the purification and partial characterization of cysteinesulfinic acid decarboxylase from porcine liver
J. Biochem. Mol. Biol.
29
335-342
1996
Sus scrofa
-
brenda
Tang, X.W.; Hsu, C.C.; Sun, Y.; Wu, E.; Yang, C.Y.; Wu, J.Y.
Multiplicity of brain cysteine sulfinic acid decarboxylase - purification, characterization and subunit structure
J. Biomed. Sci.
3
442-453
1996
Sus scrofa
brenda
Yokoyama, M.; Takeuchi, T.; Park, G.S.; Nakazoe, J.
Hepatic cysteine sulfinate decarboxylase activity in fish
Aquac. Res.
32
216-220
2001
Paralichthys olivaceus, Oncorhynchus mykiss, no activity in Seriola quinqueradiata, no activity in Thunnus thynnus, no activity in Katsuwonus pelamis
-
brenda
Park, E.; Park, S.Y.; Wang, C.; Xu, J.; LaFauci, G.; Schuller-Levis, G.
Cloning of murine cysteine sulfinic acid decarboxylase and its mRNA expression in murine tissues
Biochim. Biophys. Acta
1574
403-406
2002
Mus musculus (Q8K566), Mus musculus
brenda
Davis, K.; Foos, T.; Wu, J.Y.; Schloss, J.V.
Oxygen-induced seizures and inhibition of human glutamate decarboxylase and porcine cysteine sulfinic acid decarboxylase by oxygen and nitric oxide
J. Biomed. Sci.
8
359-364
2001
Sus scrofa
brenda
Park, T.; Rogers, Q.R.
Hepatic and renal cysteine sulfinic acid decarboxylase activities in cats fed different levels of dietary protein and taurine
J. Food Sci. Nutr.
4
47-51
1999
Felis catus
-
brenda
Reymond, I.; Bitoun, M.; Levillain, O.; Tappaz, M.
Regional expression and histological localization of cysteine sulfinate decarboxylase mRNA in the rat kidney
J. Histochem. Cytochem.
48
1461-1468
2000
Rattus norvegicus
brenda
Eppler, B.; Dawson, R.Jr.
Cysteine sulfinate decarboxylase and cysteine dioxygenase activities do not correlate with strain-specific changes in hepatic and cerebellar taurine content in aged rats
Mech. Ageing Dev.
110
57-72
1999
Rattus norvegicus
brenda
Li, J.H.; Ling, Y.Q.; Fan, J.J.; Zhang, X.P.; Cui, S.
Expression of cysteine sulfinate decarboxylase (CSD) in male reproductive organs of mice
Histochem. Cell Biol.
125
607-613
2005
Mus musculus
brenda
Skoldberg, F.; Rorsman, F.; Perheentupa, J.; Landin-Olsson, M.; Husebye, E.S.; Gustafsson, J.; Kampe, O.
Analysis of antibody reactivity against cysteine sulfinic acid decarboxylase, a pyridoxal phosphate-dependent enzyme, in endocrine autoimmune disease
J. Clin. Endocrinol. Metab.
89
1636-1640
2004
Homo sapiens (Q9Y600), Homo sapiens
brenda
Ko, K.S.; Torres, C.L.; Fascetti, A.J.; Stipanuk, M.H.; Hirschberger, L.; Rogers, Q.R.
Copper deficiency does not lead to taurine deficiency in rats
J. Nutr.
136
2502-2505
2006
Rattus norvegicus
brenda
Ueki, I.; Stipanuk, M.H.
Enzymes of the taurine biosynthetic pathway are expressed in rat mammary gland
J. Nutr.
137
1887-1894
2007
Rattus norvegicus
brenda
Ueki, I.; Stipanuk, M.H.
3T3-L1 adipocytes and rat adipose tissue have a high capacity for taurine synthesis by the cysteine dioxygenase/cysteinesulfinate decarboxylase and cysteamine dioxygenase pathways
J. Nutr.
139
207-214
2009
Mus musculus
brenda
Honjoh, K.I.; Matsuura, K.; Machida, T.; Nishi, K.; Nakao, M.; Yano, T.; Miyamoto, T.; Iio, M.
Enhancement of menadione stress tolerance in yeast by accumulation of hypotaurine and taurine: co-expression of cDNA clones, from Cyprinus carpio, for cysteine dioxygenase and cysteine sulfinate decarboxylase in Saccharomyces cerevisiae
Amino Acids
38
1173-1183
2009
Cyprinus carpio (Q2PFL0), Cyprinus carpio
brenda
Yang, J.; Wu, G.; Feng, Y.; Sun, C.; Lin, S.; Hu, J.
CSD mRNA expression in rat testis and the effect of taurine on testosterone secretion
Amino Acids
39
155-160
2009
Rattus norvegicus
brenda
Fan, J.J.; Zhou, J.L.; Li, J.H.; Cui, S.
Accessory sex glands of male mice have the ability to synthesize taurine via the cysteine sulfinate decarboxylase pathway
Cell Biol. Int.
33
684-689
2009
Mus musculus
brenda
Liu, P.; Torrens-Spence, M.P.; Ding, H.; Christensen, B.M.; Li, J.
Mechanism of cysteine-dependent inactivation of aspartate/glutamate/cysteine sulfinic acid alpha-decarboxylases
Amino Acids
44
391-404
2013
Homo sapiens
brenda
Chang, Y.C.; Ding, S.T.; Lee, Y.H.; Wang, Y.C.; Huang, M.F.; Liu, I.H.
Taurine homeostasis requires de novo synthesis via cysteine sulfinic acid decarboxylase during zebrafish early embryogenesis
Amino Acids
44
615-629
2013
Danio rerio (Q5U3I6), Danio rerio
brenda
Kerr, T.; Matsumoto, Y.; Matsumoto, H.; Xie, Y.; Hirschberger, L.; Stipanuk, M.; Anakk, S.; Moore, D.; Watanabe, M.; Kennedy, S.; Davidson, N.
Cysteine sulfinic acid decarboxylase regulation: A role for farnesoid X receptor and small heterodimer partner in murine hepatic taurine metabolism
Hepatol. Res.
44
E218-228
2014
Mus musculus
brenda
Saenko, S.V.; Jeronimo, M.A.; Beldade, P.
Genetic basis of stage-specific melanism: a putative role for a cysteine sulfinic acid decarboxylase in insect pigmentation
Heredity
108
594-601
2012
Bicyclus anynana (G8FGR5), Bicyclus anynana
brenda
Liu, P.; Ding, H.; Christensen, B.M.; Li, J.
Cysteine sulfinic acid decarboxylase activity of Aedes aegypti aspartate 1-decarboxylase: the structural basis of its substrate selectivity
Insect Biochem. Mol. Biol.
42
396-403
2012
Aedes aegypti
brenda
Nagasaki, T.; Hongo, Y.; Koito, T.; Nakamura-Kusakabe, I.; Shimamura, S.; Takaki, Y.; Yoshida, T.; Maruyama, T.; Inoue, K.
Cysteine dioxygenase and cysteine sulfinate decarboxylase genes of the deep-sea mussel Bathymodiolus septemdierum possible involvement in hypotaurine synthesis and adaptation to hydrogen sulfide
Amino Acids
47
571-578
2015
Bathymodiolus septemdierum (A0A0A8J1X6), Bathymodiolus septemdierum
brenda
Haga, Y.; Kondo, H.; Kumagai, A.; Satoh, N.; Hirono, I.; Satoh, S.
Isolation, molecular characterization of cysteine sulfinic acid decarboxylase (CSD) of red sea bream Pagrus major and yellowtail Seriola quinqueradiata and expression analysis of CSD from several marine fish species
Aquaculture
449
8-17
2015
Anguilla japonica, Cyprinus carpio (Q2PFL0), Danio rerio (Q5U3I6), Gasterosteus aculeatus (G3P4S6), Lateolabrax japonicus, Oryzias latipes (H2LVH5), Pagrus major (A0A0N9E6Z6), Seriola quinqueradiata (A0A0N9E6M5), Takifugu rubripes (Q1KKU1), Tetraodon nigroviridis (H3DC51), Verasper moseri
-
brenda
Liu, S.; Liu, Y.; Ma, Q.; Cui, S.; Liu, J.
Expression and localization of cysteine sulfinate decarboxylase in major salivary glands of male mice
Arch. Oral Biol.
60
615-621
2015
Mus musculus (Q9DBE0)
brenda
Deng, J.; Wu, Q.; Gao, H.; Ou, Q.; Wu, B.; Yan, B.; Jiang, C.
Molecular characterization and directed evolution of a metagenome-derived L-cysteine sulfinate decarboxylase
Food Technol. Biotechnol.
56
117-123
2018
unidentified prokaryotic organism (A0A2I9)
brenda
Park, E.; Park, S.Y.; Dobkin, C.; Schuller-Levis, G.
Development of a novel cysteine sulfinic acid decarboxylase knockout mouse dietary taurine reduces neonatal mortality
J. Amino Acids
2014
346809
2014
Mus musculus (Q9DBE0), Mus musculus, Mus musculus C57BL/6 (Q9DBE0)
brenda
Zhao, X.; Li, Q.; Meng, Q.; Yue, C.; Xu, C.
Identification and expression of cysteine sulfinate decarboxylase, possible regulation of taurine biosynthesis in Crassostrea gigas in response to low salinity
Sci. Rep.
7
5505
2017
Magallana gigas (A0A221J366), Magallana gigas (A0A221J378)
brenda
Raasakka, A.; Mahootchi, E.; Winge, I.; Luan, W.; Kursula, P.; Haavik, J.
Structure of the mouse acidic amino acid decarboxylase GADL1
Acta Crystallogr. F Struct. Biol. Commun.
74
65-73
2018
Mus musculus (Q80WP8)
brenda
Liu, Z.; Zheng, W.; Ye, W.; Wang, C.; Gao, Y.; Cui, W.; Zhou, Z.
Characterization of cysteine sulfinic acid decarboxylase from Tribolium castaneum and its application in the production of beta-alanine
Appl. Microbiol. Biotechnol.
103
9443-9453
2019
Tribolium castaneum (A7U8C7)
brenda
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