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Information on EC 4.3.1.17 - L-serine ammonia-lyase
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4.3.1.17 L-serine ammonia-lyaseIUBMB Comments
Most enzymes that catalyse this reaction are pyridoxal-phosphate-dependent, although some enzymes contain an iron-sulfur cluster instead . The reaction catalysed by both types of enzymes involves the initial elimination of water to form an enamine intermediate (hence the enzyme's original classification as EC 4.2.1.13, L-serine dehydratase), followed by tautomerization to an imine form and hydrolysis of the C-N bond. The latter reaction, which can occur spontaneously, is also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. This reaction is also carried out by EC 4.3.1.19, threonine ammonia-lyase, from a number of sources.
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Word Map
- 4.3.1.17
- aminotransferase
- pyridoxal
-
deamination
- glucagon
-
gluconeogenesis
- hydroxymethyltransferase
-
gluconeogenic
- l-isoleucine
- d-serine
-
plp-dependent
-
peptostreptococcus
- 2-oxobutyrate
- deaminases
- asaccharolyticus
- analysis
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
bsLSD type 1, cSDH, Dehydratase, L-serine, EC 4.2.1.13, GSU0486, HSDH, L-Hydroxy amino acid dehydratase, L-SD, L-SD1, L-SD2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Dehydratase, L-serine
-
-
-
-
EC 4.2.1.13
-
-
formerly
-
GSU0486
HSDH
L-Hydroxy amino acid dehydratase
-
-
-
-
L-SD
L-SD1
-
-
-
-
L-SD2
-
-
-
-
L-serine ammonia-lyase
L-Serine deaminase
L-serine dehydratase
L-threonine deaminase
L-threonine dehydratase
SD
-
-
-
-
SDH
Serine deaminase
Serine dehydratase
tdcB
TdcG
additional information
-
L-serine dehydratase and cystathionine beta-synthase are the same enzyme
L-SD
-
-
-
-
L-Serine deaminase
-
-
-
-
SDH
-
-
-
-
Serine deaminase
-
-
-
-
Serine dehydratase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-aminoprop-2-enoate = 2-iminopropanoate
(1b), spontaneous
-
-
-
2-iminopropanoate + H2O = pyruvate + NH3
(1c), spontaneous
-
-
-
L-serine = 2-aminoprop-2-enoate + H2O
(1a)
-
-
-
L-serine = pyruvate + NH3
A pyridoxal-phosphate protein. This reaction is also carried out by EC 4.3.1.19 threonine ammonia-lyase, from a number of sources. The reaction catalysed probably involves initial elimination of water, hence the enzyme's original classification as EC 4.2.1.13, L-serine dehydratase, followed by isomerization and hydrolysis of the product with C-N bond breakage
-
-
-
L-serine = pyruvate + NH3
A pyridoxal-phosphate protein.
-
-
-
L-serine = pyruvate + NH3
reaction analysis by ab initio quantum mechanical/molecular mechanical method, the reaction involves a Schiff base formation step and a proton-relaying mechanism involving the phosphate of the cofactor in the beta-hydroxyl-leaving step following sequentially after the elimination of the alpha-proton, leading to a single but sequential alpha,beta-elimination step. The rate-limiting transition state is specifically stabilized by the enzyme environment, catalytic mechanism involving Lys41 in the active site, detailed overview
L-serine = pyruvate + NH3
(overall reaction)
-
-
-
L-serine = pyruvate + NH3
pre-steady-state kinetic analysis of L-serine binding to lpLSD demonstrates that L-serine binds to a second noncatalytic site and produces a conformational change in the enzyme. The rate of this conformational change is too slow for its participation in the catalytic cycle but rather occurs prior to catalysis to produce an activated form of the enzyme
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
elimination
-
-
beta-position of amino acid
-
elimination
-
-
alpha,beta-position of amino acid
-
elimination
-
-
of NH3, alpha,beta-position of amino acid, C-N bond cleavage, C-O bond cleavage
-
elimination
-
-
of NH3, alpha,beta-position of amino acid
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
L-serine ammonia-lyase (pyruvate-forming)
Most enzymes that catalyse this reaction are pyridoxal-phosphate-dependent, although some enzymes contain an iron-sulfur cluster instead [6]. The reaction catalysed by both types of enzymes involves the initial elimination of water to form an enamine intermediate (hence the enzyme's original classification as EC 4.2.1.13, L-serine dehydratase), followed by tautomerization to an imine form and hydrolysis of the C-N bond. The latter reaction, which can occur spontaneously, is also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. This reaction is also carried out by EC 4.3.1.19, threonine ammonia-lyase, from a number of sources.
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CAS REGISTRY NUMBER
COMMENTARY
9014-27-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-allo-threonine
2-oxobutyrate + NH3
-
at 4.6% of the rate with L-serine
-
-
?
L-threonine
3-hydroxy-2-butenoic acid + NH3
-
alpha,beta-elimination reaction
-
-
?
L-Leu
3-Hydroxy-2-oxopropionate + NH3
-
3% of the activity with L-Ser
-
-
?
L-Leu
3-Hydroxy-2-oxopropionate + NH3
-
3% of the activity with L-Ser
-
-
?
L-serine
pyruvate + NH3
-
specific for L-Ser
-
?
L-serine
pyruvate + NH3
SDH is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes dehydration of L-Ser/Thr to yield pyruvate/ketobutyrate and ammonia
-
-
?
L-serine
pyruvate + NH3
a rigid pyridine ring pocket is necessary for cSDH having a flexible substrate binding-loop
-
-
?
L-serine
pyruvate + NH3
wild-type enzyme shows almost no activity with D-serine
-
-
?
L-Thr
2-oxobutanoate + NH3
-
1% of the activity with L-Ser
-
-
?
L-Thr
2-oxobutanoate + NH3
-
1% of the activity with L-Ser
-
-
?
L-Thr
2-oxobutanoate + NH3
Km -value is approximately 150 times that for L-serine. At an L-threonine concentration of 300 mM, the enzyme activity is approximately 5% of the activity for L-serine at its Km of 2 mM
-
-
?
additional information
?
-
-
no substrate: D-serine. Extremely poor substrate: L-cysteine
-
-
?
additional information
?
-
-
GSU0486 mainly catalyzes the deamination of L-threonine, EC 4.3.1.19
-
-
?
additional information
?
-
Geobacter sulfurreducens ATCC 51573 / DSM 12127
-
GSU0486 mainly catalyzes the deamination of L-threonine, EC 4.3.1.19
-
-
?
additional information
?
-
-
GSU0486 mainly catalyzes the deamination of L-threonine, EC 4.3.1.19
-
-
?
additional information
?
-
enzyme shows homotopic cooperativity, Hill coefficient of wild-type is 1.7
-
-
?
additional information
?
-
-
enzyme shows homotopic cooperativity, Hill coefficient of wild-type is 1.7
-
-
?
additional information
?
-
racemization and elimination activities reside at the same active site of enzyme. Racemization activity is specific to serine, elimination activity has a broader specificity for L-amino acids with a suitable leaving group at the beta-carbon
-
-
?
additional information
?
-
-
ration of elimination reaction/racemization reaction for substrate L-serine is 3.7
-
-
?
additional information
?
-
cytotoxic early protein 77 of mycobacteriophage L5 interacts with MSMEG_3532
-
-
?
additional information
?
-
-
cytotoxic early protein 77 of mycobacteriophage L5 interacts with MSMEG_3532
-
-
?
additional information
?
-
the enzyme does not show 1-aminocyclopropane-1-carboxylate deaminase activity at high temperature as well as at room temperature though it has significant sequence similarity to 1-aminocyclopropane-1-carboxylate deaminase from the yeast Hansenula saturnus
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-serine
pyruvate + NH3
SDH is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes dehydration of L-Ser/Thr to yield pyruvate/ketobutyrate and ammonia
-
-
?
additional information
?
-
cytotoxic early protein 77 of mycobacteriophage L5 interacts with MSMEG_3532
-
-
?
additional information
?
-
-
cytotoxic early protein 77 of mycobacteriophage L5 interacts with MSMEG_3532
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
K+ and NH4+ decrease the dissociation constant of pyridoxal 5'-phosphate. Tris and the substrate compete for pyridoxal 5'-phosphate with the enzyme because of Schiff's base formation. Influence of substrate concentration on the Km-value of pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
one mol of enzyme contains two mol of pyridoxal phosphate
pyridoxal 5'-phosphate
-
pyridoxal-5'-phosphate-independent enzyme
pyridoxal 5'-phosphate
-
pyridoxal-5'-phosphate-independent enzyme
pyridoxal 5'-phosphate
-
pyridoxal-5'-phosphate-independent enzyme
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate is sandwiched between F40 and A222
pyridoxal 5'-phosphate
SDH is a pyridoxal 5'-phosphate-dependent enzyme, PLP is covalently attached to K48 by Schiff-base linkage in the active site. The ring nitrogen of PLP is involved in a H-bonding with C309, but is apparently not protonated
pyridoxal 5'-phosphate
cofactor is located in the crevice between the two domains, attached to residue Lys52 by a Schiff-base linkage
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4Fe-4S-center
the enzyme contains a [4Fe-4S]2+ cluster that acts as a Lewis acid to extract the hydroxyl group of L-serine during the dehydration reaction. Fe-S cluster binding induces protein conformational changes in L-serine dehydratase. All four iron atoms of the [4Fe-4S] cluster are coordinated with protein cysteine residues (C396, C485, C343, C385). formation of disulfide bonds between C396 and C485 and possibly between C343 and C385
Ca2+
Fe2+
Iron
K+
KCl
-
nonspecific requirement for a monovalent or bivalent cation. Half-maximal activity is produced with 22.5 mM KCl
Mg2+
MgCl2
Mn2+
Iron
-
7.7 mol iron per mol dimer, two (4Fe-4S)2+ clusters per dimer in anaerobically isolated enzyme, exposure to air results in loss of clusters and concomitant loss of enzyme activity
Iron
-
presence of (4Fe-4S)2+ and of (2Fe-2S)2+ clusters involved in catalytic turnover
Iron
-
enzyme probably contains a diamagnetic [4Fe-4S]2+cluster which is converted by oxidation and loss of iron ion to a paramegnetic [3Fe-4S]+cluster resulting in inactivation of the enzyme
Iron
-
the enzyme contains 3.8 mol Fe and 5.6 mol inorganic sulfur per mol of heterodimer, indicating the presence of an [Fe-S]center
MgCl2
-
nonspecific requirement for a monovalent or bivalent cation. Half-maximal activity with 1.0 mM MgCl2
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
homocysteine
-
noncompetitive with respect to substrate, competitive with regard to pyridoxal 5'-phosphate
NH4Cl
-
significant fall in the serine-dehydratase expression during experimental chronic acidosis, acidosis is induced by ingestion of 0.28 M ammonium chloride solution
ATP
-
inhibitory to L-serine O-sulfate dehydration reaction, activating for racemization reraction
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
leucine
excess leucine intake strongly induces SDH activity in the liver but not in the kidney
additional information
-
the enzyme is inactive in crude extract and can be activated with iron and dithiothreitol. The activation requires oxygen, and is inhibited by free radical scavengers and by diethylenentriamine pentaacetic acid, which prevents Fe cycling
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acidosis
Downregulation in the expression of the serine dehydratase in the rat liver during chronic metabolic acidosis.
Acidosis
Localization and hormonal control of serine dehydratase during metabolic acidosis differ markedly from those of phosphoenolpyruvate carboxykinase in rat kidney.
Carcinoma, Hepatocellular
Effect of B6 deficiency on hepatoma 7794A growth rate: activities of tyrosine transaminase and serine dehydratase before and after induction by hydrocortisone.
Carcinoma, Hepatocellular
Effect of pyridoxine availability on the activity of serine dehydratase of normal liver, host liver, and three Morris hepatomas.
Carcinoma, Hepatocellular
Expression of only one of two types of mRNA transcribed from the serine dehydratase gene is repressed in hepatoma cells.
Carcinoma, Hepatocellular
Hormonal and nutritional effects on the binding of 125I-labeled anti-serine dehydratase Fab' to rat tissue polysomes.
Carcinoma, Hepatocellular
Metabolic adaptations in rat hepatomas: altered regulation of serine dehydratase synthesis by glucose and amino acids in hepatocellular carcinomas.
Dehydration
A catalytic mechanism that explains a low catalytic activity of serine dehydratase like-1 from human cancer cells: crystal structure and site-directed mutagenesis studies.
Dehydration
Hydrogen-Deuterium Exchange Mass Spectrometry Reveals Unique Conformational and Chemical Transformations Occurring upon [4Fe-4S] Cluster Binding in the Type 2 l-Serine Dehydratase from Legionella pneumophila.
Diabetes Mellitus
Regulation of the expression of the serine dehydratase gene in the kidney and liver of the rat.
Diabetic Foot
Enzymatically active Peptostreptococcus magnus: association with site of infection.
Fragile X Syndrome
Identification of distinct genes with restricted expression in the somitic mesoderm in Xenopus embryo.
Hepatitis
[The activity of serine dehydratase enzyme of liver tissue in experimental murine infection with mouse hepatitis virus 3]
Hyperinsulinism
Effects of insulin, epinephrine, and glucose on regulation of transcription of the serine dehydratase gene in newborn dogs.
Hypersensitivity
Nutritional regulation and tissue-specific expression of the serine dehydratase gene in rat.
Hypersensitivity
Threonine deaminase from Escherichia coli: feedback-hypersensitive enzyme from a genetic regulatory mutant.
Infections
Enzymatically active Peptostreptococcus magnus: association with site of infection.
Infections
[The activity of serine dehydratase enzyme of liver tissue in experimental murine infection with mouse hepatitis virus 3]
Intellectual Disability
Identification of distinct genes with restricted expression in the somitic mesoderm in Xenopus embryo.
Neoplasms
A catalytic mechanism that explains a low catalytic activity of serine dehydratase like-1 from human cancer cells: crystal structure and site-directed mutagenesis studies.
Neoplasms
Induction of enzymes by glucagon, glucose repression, adenosine 3',5'-monophosphate concentration during carcinogenesis and in Morris 6918A hepatoma.
Starvation
Control of hepatic utilization of serine, glycine and threonine in fed and starved rats.
Starvation
Distribution of amino acids and amino-acid enzymes in whole kidney and renal cortex. Effect of 24-h starvation.
Starvation
Effects of glucose, insulin, and cAMP on transcription of the serine dehydratase gene in rat liver.
Starvation
Regulation of the expression of the serine dehydratase gene in the kidney and liver of the rat.
Starvation
Serine dehydratase and tyrosine aminotransferase activities increased by long-term starvation and recovery by refeeding in rainbow trout (Oncorhynchus mykiss).
Starvation
Synthesis of inducible enzyme in Escherichia coli recovering from prolonged energy starvation.
Starvation
The regulation of serine dehydratase and glucose-6-phosphatase in hyperplastic nodules of rat liver during diethylnitrosamine and N-2-fluorenylacetamide feeding.
Tuberculosis
Kinetic Evidence of a Noncatalytic Substrate Binding Site That Regulates Activity in Legionella pneumophilal-Serine Dehydratase.
Tuberculosis
Kinetic, mutagenic, and structural homology analysis of L-serine dehydratase from Legionella pneumophila.
Tuberculosis
Loop-mediated isothermal amplification as alternative to PCR for the diagnosis of extra-pulmonary tuberculosis.
Tuberculosis
Structure of L-serine dehydratase from Legionella pneumophila: novel use of the C-terminal cysteine as an intrinsic competitive inhibitor.
Vitamin B 12 Deficiency
Vitamin B12 deficiency results in the abnormal regulation of serine dehydratase and tyrosine aminotransferase activities correlated with impairment of the adenylyl cyclase system in rat liver.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.49
L-serine O-sulfate
pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction
12
D-serine
-
mutant Q155D, alpha,beta-elimination, presence of ATP, pH 7.4, 37°C
55
D-threonine
-
wild-type, alpha,beta-elimination, presence of ATP, pH 7.4, 37°C
60
D-threonine
-
mutant Q155D, alpha,beta-elimination, presence of ATP, pH 7.4, 37°C
2
L-Ser
wild-type, pH 7.0, temperature not specified in the publication
2.2
L-Ser
mutant C183A, pH 7.0, temperature not specified in the publication
2.7
L-Ser
mutant C226A, pH 7.0, temperature not specified in the publication
3
L-Ser
mutant C221A, pH 7.0, temperature not specified in the publication
6.9
L-Ser
mutant C458A, pH 7.0, temperature not specified in the publication
17.8
L-Ser
mutant C304A, pH 7.0, temperature not specified in the publication
0.00258
L-serine
pH 7, temperature not specified in the publication, Vmax: 11.7/min/mg
1.7
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme T57A
2
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme S17A
2
L-serine
pH 7.0, temperature not specified in the publication, native enzyme
2.3
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme E457A
3 - 3.2
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme H124A/N126A
3.1
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme T290A
3.5
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme S53A
4.7
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme T20A
5.1
L-serine
pH 7, temperature not specified in the publication
6.9
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme C458A
11
L-serine
-
mutant Q155D, alpha,beta-elimination, presence of ATP, pH 7.4, 37°C
13.6
L-serine
-
pH 7, temperature not specified in the publication, 100 mM KCl
24.4
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme H19A
25.5
L-serine
-
pH 7, temperature not specified in the publication, 300 mM KCl
29.2
L-serine
-
pH 7, temperature not specified in the publication, 500 mM KCl
182
L-serine
-
pH 7.4, 25°C, animals treated with thioacetamide for 97 days
189
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme T446A
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.6
beta-chloro-L-alanine
pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction
0.49
L-serine O-sulfate
pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction
31
L-threo-3-hydroxyaspartate
pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction
0.012
D-serine
-
mutant Q155D, alpha,beta-elimination, presence of ATP, pH 7.4, 37°C
0.042
D-serine
-
wild-type, alpha,beta-elimination, presence of ATP, pH 7.4, 37°C
0.028
D-threonine
-
mutant Q155D, alpha,beta-elimination, presence of ATP, pH 7.4, 37°C
0.3
D-threonine
-
wild-type, alpha,beta-elimination, presence of ATP, pH 7.4, 37°C
323
L-Ser
mutant C304A, pH 7.0, temperature not specified in the publication
330
L-Ser
wild-type, pH 7.0, temperature not specified in the publication
359
L-Ser
mutant C221A, pH 7.0, temperature not specified in the publication
467
L-Ser
mutant C226A, pH 7.0, temperature not specified in the publication
506
L-Ser
mutant C183A, pH 7.0, temperature not specified in the publication
512
L-Ser
mutant C458A, pH 7.0, temperature not specified in the publication
0.166
L-serine
-
wild-type, alpha,beta-elimination, presence of ATP, pH 7.4, 37°C
4.07
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme T290A
8.8
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme T57A
31
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme H19A
67
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme S17A
112
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme H124A/N126A
181
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme T20A
184
L-serine
-
pH 7, temperature not specified in the publication, 100 mM KCl
201
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme S53A
249
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme E457A
286
L-serine
pH 7, temperature not specified in the publication
330
L-serine
pH 7.0, temperature not specified in the publication, native enzyme
356
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme T446A
465
L-serine
-
pH 7, temperature not specified in the publication, 300 mM KCl
512
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme C458A
585
L-serine
-
pH 7, temperature not specified in the publication, 500 mM KCl
10.5
L-threonine
pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
18
L-Ser
mutant C304A, pH 7.0, temperature not specified in the publication
74
L-Ser
mutant C458A, pH 7.0, temperature not specified in the publication
120
L-Ser
mutant C221A, pH 7.0, temperature not specified in the publication
170
L-Ser
mutant C226A, pH 7.0, temperature not specified in the publication
170
L-Ser
wild-type, pH 7.0, temperature not specified in the publication
230
L-Ser
mutant C183A, pH 7.0, temperature not specified in the publication
1.3
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme H19A
1.3
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme T290A
1.8
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme T446A
3.4
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme H124A/N126A
5.2
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme T57A
14
L-serine
-
pH 7, temperature not specified in the publication, 100 mM KCl
18
L-serine
-
pH 7, temperature not specified in the publication, 300 mM KCl
20
L-serine
-
pH 7, temperature not specified in the publication, 500 mM KCl
34
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme S17A
39
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme T20A
57
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme S53A
74
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme C458A
108
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme E457A
165
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme S16A
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10
D-serine
pH 7.0, temperature not specified in the publication
0.1
L-cysteine
pH 7.0, temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0006
0.0008
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.3
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
6.5 - 9.5
-
pH 6.5: about 40% of maximal activity, pH 9.5: about 90% of maximal activity
7 - 9.5
-
pH 7: about 35% of maximal activity, pH 9.5: about 35% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
40
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18 - 50
-
18°C: about 50% of maximal activity, 50°C: about 25% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional enzyme, racemization of serine and elimination of L-serine and L-serine-O-sulfate to form pyruvate
-
-
brenda
bifunctional enzyme, racemization of serine and elimination of L-serine and L-serine-O-sulfate to form pyruvate
Swissprot
brenda
bifunctional enzymes, racemization of serine and alpha,beta-elimination of L-serine
-
-
brenda
isoforms A and B, bifunctional enzymes, racemization of serine and elimination of L-serine and L-serine-O-sulfate to form pyruvate
-
-
brenda
includes 4.3.1.17 and 4.3.1.19; male Sprague-Dawley rat
UniProt
brenda
SDH activity and its gene expression are induced in both growing and mature rats when their protein intake exceeds their nutrintional requirements
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
enzyme activity increases with age of animals and also in response to the amount of surplus amino acids from dietary protein. Induction is mainly controlled at the level of transcription and seems not to be related to gluconeogenesis
brenda
-
suffering chronic injury caused by ingestion of thioacetamide. After 97 days of intake, enzyme activity is about 60% lower than in controls. No significant differences in Km-value are found, while enzyme protein level is reduced. Enzyme is localized to periportal zone of the hepatic acinus
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
Escherichia coli K-12 provided with glucose and a mixture of amino acids depletes L-serine more quickly than any other amino acid even in the presence of ammonium sulfate. A mutant lacking 4Fe4S L-serine deaminases SdaA, SdaB, and TdcG is unable to do this. The high level of L-serine that accumulates when the mutant is exposed to amino acid mixtures starves the cells for C1 units and interferes with cell wall synthesis. Growth in minimal medium containing glucose, ammonium sulfate, and Casamino Acids results in deformed cells and frequently lysing, which can be reversed by adding S-adenosylmethionine
physiological function
cytotoxic early protein 77 of mycobacteriophage L5 interacts with MSMEG_3532
Show AA Sequence and Transmembrane Helices (37154 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10000
-
1 * 26000 + 1 * 10000, enzyme either exists as a heterooctamer or a heterodimer, SDS-PAGE
25000
26000
30000
34000
40000
46000
-
2 * 52910, calculated for His-tagged protein, 2 * 48460, calculated for native protein, 2 * 46000, SDS-PAGE of His-tagged protein
48460
-
2 * 52910, calculated for His-tagged protein, 2 * 48460, calculated for native protein, 2 * 46000, SDS-PAGE of His-tagged protein
49476
52910
-
2 * 52910, calculated for His-tagged protein, 2 * 48460, calculated for native protein, 2 * 46000, SDS-PAGE of His-tagged protein
57000
60000
66000
25000
-
1 * 25000 + 1 * 30000, the enzyme is composed of two different subunits in a 1:1 stoichiometry, forming heterodimers to heterooctamers
25000
-
2 * 25000 + 2 * 30000, the enzyme is composed of two different subunits in a 1:1 stoichiometry, forming heterodimers to heterooctamers
25000
-
3 * 25000 + 3 * 30000, the enzyme is composed of two different subunits in a 1:1 stoichiometry, forming heterodimers to heterooctamers
25000
-
4 * 25000 + 4 * 30000, the enzyme is composed of two different subunits in a 1:1 stoichiometry, forming heterodimers to heterooctamers
26000
-
1 * 26000 + 1 * 10000, enzyme either exists as a heterooctamer or a heterodimer, SDS-PAGE
26000
-
4 * 26000 + 4 * 30000, enzyme either exists as a heterooctamer or a heterodimer, SDS-PAGE
30000
-
1 * 25000 + 1 * 30000, the enzyme is composed of two different subunits in a 1:1 stoichiometry, forming heterodimers to heterooctamers
30000
-
2 * 25000 + 2 * 30000, the enzyme is composed of two different subunits in a 1:1 stoichiometry, forming heterodimers to heterooctamers
30000
-
3 * 25000 + 3 * 30000, the enzyme is composed of two different subunits in a 1:1 stoichiometry, forming heterodimers to heterooctamers
30000
-
4 * 25000 + 4 * 30000, the enzyme is composed of two different subunits in a 1:1 stoichiometry, forming heterodimers to heterooctamers
30000
-
4 * 26000 + 4 * 30000, enzyme either exists as a heterooctamer or a heterodimer, SDS-PAGE
49476
-
gel filtration, 1 * 49476, monomeric form does not possess enzymatic activity
49476
-
gel filtration, 2 * 49476, only dimer displays catalytic activity. In the absence of substrate, lpLSD is predominately a dimer
57000
-
gel filtration in presence of 10 mM Fe2+, dimeric enzyme form
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
-
3 * 25000 + 3 * 30000, the enzyme is composed of two different subunits in a 1:1 stoichiometry, forming heterodimers to heterooctamers
monomer
octamer
tetramer
additional information
dimer
-
1 * 26000 + 1 * 10000, enzyme either exists as a heterooctamer or a heterodimer, SDS-PAGE
dimer
-
2 * 52910, calculated for His-tagged protein, 2 * 48460, calculated for native protein, 2 * 46000, SDS-PAGE of His-tagged protein
dimer
-
gel filtration, 2 * 49476, only dimer displays catalytic activity. In the absence of substrate, lpLSD is predominately a dimer
dimer
-
1 * 25000 + 1 * 30000, the enzyme is composed of two different subunits in a 1:1 stoichiometry, forming heterodimers to heterooctamers
monomer
-
gel filtration, 1 * 49476, monomeric form does not possess enzymatic activity
octamer
-
4 * 26000 + 4 * 30000, enzyme either exists as a heterooctamer or a heterodimer, SDS-PAGE
octamer
-
4 * 25000 + 4 * 30000, the enzyme is composed of two different subunits in a 1:1 stoichiometry, forming heterodimers to heterooctamers
tetramer
-
2 * 25000 + 2 * 30000, the enzyme is composed of two different subunits in a 1:1 stoichiometry, forming heterodimers to heterooctamers
additional information
structure analysis and comparison to the rat and the human liver isozymes, the cancer cell isozyme and the liver isozyme show different active site surface amino acid residues, overview
additional information
-
structure analysis and comparison to the rat and the human liver isozymes, the cancer cell isozyme and the liver isozyme show different active site surface amino acid residues, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure obtained by molecular replacement shows a homodimer and a fold typical for beta-family pyridoxal 5'-phosphate-dependent enzymes. Each monomer serves as an active unit
-
hanging-drop vapour diffusion, 0.002 ml protein solution containing 20-30 mg/ml SDH in 20 mM Tris-HCl, pH 7.6 and 150 mM NaCl is mixed with 0.002 ml reservoir solution containing 800 mM ammonium sulfate in 100 mM Tris-HCl, pH 7.0-8.0, crystals diffract to 2.5 A
-
purified recombinant cSDH, hanging drop vapour diffusion method, 10 mg/ml protien in 50 mM Na-citrate, pH 5.6, 10 mM DL-O-methylserine, 200 mM potassium acetate, 5 mM dithiothreitol, 15% w/v PEG-8000 at 21°C, 1 week, X-ray diffraction structure determination and analysis at 2.8 A resolution
hanging-drop vapor-diffusion method, crystal structures of the native and 1-aminocyclopropane-1-carboxylate-complexed enzyme. The crystals of native and Se-Met belong to the space group P3(2)21 with unit cell parameters of a=b= 122.3 A, c = 115.0 A, and gamma = 120°, and there are three molecules in an asymmetric unit. The crystals of the ACC complex belong to space group P1 with unit cell parameters of a = 105.8 A, b = 147.2 A, c = 149.0 A, a = 73.18, b = 90.18, and gamma = 68.48, and 24 molecules are included in an asymmetric cell
crystal structures of apo-SDH and holo-SDH, crystallized with O-methylserine, at 2.8 A and 2.6 A resolution, respectively
to 1.76 A resolution. The active site is located between the small domain and large domain, and a pyridoxal 5'-phosphate is attached to Lys52 by a Schiff-base linkage
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A65G
site-directed mutagenesis of the human liver isozyme cSDH, large structural alterations, serine binding is not affected, overview
A65S
structure of A65S hSDH mutant is determined at 1.3 A resolution. Mutant shows decreased activity (50%) with substrate L-serine compared to wild-type. Mutant shows measurable activity with substrate D-serine
A65S/V225S
double mutant shows only 10% of activity with substrate L-serine compared to wild-type (100%). Double mutant shows very little but measurable activity with substrate D-serine
C303A
site-directed mutagenesis of the human liver isozyme cSDH, structural alterations, overview
C309A
site-directed mutagenesis of the cancer cell isozyme cSDH, structural alterations, overview
G72A
site-directed mutagenesis of the cancer cell isozyme cSDH, large structural alterations, serine binding is not affected, changing alanine to glycine at residue 72 in cSDH is responsible for the reduced catalytic activity of cSDH, overview
G72A/S228A
site-directed mutagenesis of the cancer cell isozyme cSDH, catalytic activities for both the substrates are substantially recovered, overview
C183A
135% of wild-type activity. Enzyme retains the positive cooperativity seen in the native enzyme
C221A
70% of wild-type activity. Enzyme retains the positive cooperativity seen in the native enzyme
C226A
100% of wild-type activity. Enzyme retains the positive cooperativity seen in the native enzyme
C304A
10% of wild-type activity. Mutant displays altered kinetics with a higher Km and a Hill coefficient indicating negative homotropic cooperativity
C343A
inactive, mutants lacks the charge transfer absorbance at 400 nm that is indicative of the 4Fe-4S center
C385A
inactive, mutants lacks the charge transfer absorbance at 400 nm that is indicative of the 4Fe-4S center
C396A
inactive, mutants lacks the charge transfer absorbance at 400 nm that is indicative of the 4Fe-4S center
C458A
E457A
kcat/Km for L-serine is 1.5fold lower than the wild-type value
H124A/N126A
kcat/Km for L-serine is 48.5fold lower than the wild-type value
H19A
kcat/Km for L-serine is 127fold lower than the wild-type value
S17A
kcat/Km for L-serine is 4.8fold lower than the wild-type value
S53A
kcat/Km for L-serine is 2.9fold lower than the wild-type value
T20A
kcat/Km for L-serine is 4.2fold lower than the wild-type value
T290A
kcat/Km for L-serine is 127fold lower than the wild-type value
T446A
kcat/Km for L-serine is 91.7fold lower than the wild-type value
T57A
kcat/Km for L-serine is 31.7fold lower than the wild-type value
H152S
-
ratio of elimination reaction to racemization is 1.4 compared to 3.7 in wild-type
N154F
-
ratio of elimination reaction to racemization is 0.33 compared to 3.7 in wild-type
P153S
-
ratio of elimination reaction to racemization is 0.24 compared to 3.7 in wild-type
Q155D
-
ratio of elimination reaction to racemization is 0.25 compared to 3.7 in wild-type
additional information
-
construction of a mutant strain devoid of functional genes sdaA, sdaB, tdcG encoding the three isozymes of the organism, the loss of the ability to deaminate L-serine severely impairs growth and cell division in Escherichia coli K-12 leading e.g. to filamentation, phenotype, overview
C458A
44% of wild-type activity. Enzyme retains the positive cooperativity seen in the native enzyme
C458A
kcat/Km for L-serine is 2.2fold lower than the wild-type value
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
complete loss of activity within 30 min. Fe2+, L-Ser D-Ser or ethanolamine decrease the loss of activity at 37°C
40
45
50
55
55
-
complete loss of activity after 4 min. NH4Cl, KCl or (NH4)2SO4 stabilize
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
it is absolutely critical that dilutions of the purified enzyme be made in buffer containing 50% glycerol, otherwise the enzyme rapidly loses activity
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
complete loss of activity in crude extracts after exposure to air for 1 h
-
650851
inactivated upon exposure to air, reactivated by Fe2+ under aerobic conditions
purified SdaA is inactivated with a half-life of approx. 1.5 h upon exposure to air, inactivated SdaA can be reactivated to approx. 60% of its activity under strict anaerobic conditiones with Fe2+ and dithiothreitol
-
651494
rapid loss of activity upon exposure to air, reactivation by Fe2+
inactivated upon exposure to air, reactivated by Fe2+ under aerobic conditions
-
210790
inactivated upon exposure to air, reactivated by Fe2+ under aerobic conditions
-
210791
rapid loss of activity upon exposure to air, reactivation by Fe2+
-
210794
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 40% loss of activity after 24 h, 0.76 mg/ml protein concentration, partially purified enzyme
-
-20°C, pH 7.0-8.0, stable over many months, enzyme in crude extract
-
-70°C, 0.6 mg/ml protein, 30% loss of activity after 1 month, purified enzyme
-
4°C, 90% loss of activity after 24 h, 0.76 mg/ml protein concentration, partially purified enzyme
-
unstable within the cell in the presence of its inducers, Gly and Leu, but not in their absence
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
anaerobic purification of His-tagged enzyme, purified protein is brown in colour
-
expression in Escherichia coli with N-terminal His-tag, purification protocol from inclusion bodies
-
partial
proteins of crude extracts are fractionated using a DEAE-Sephadex A-25 column
recombinant cancer cell isozyme cSDH to homogeneity by ammonium sulfate fractionation, dialysis, anion exchange and nickel affinity chromatography
recombinant protein expressed in Escherichia coli
recombinant SDH
use of gene fusion of the structural gene sdaA to purify L-serine deaminase 1
-
using cobalt-based affinity columns
using Ni-NTA chromatography
proteins of crude extracts are fractionated using a DEAE-Sephadex A-25 column
-
proteins of crude extracts are fractionated using a DEAE-Sephadex A-25 column
-
proteins of crude extracts are fractionated using a DEAE-Sephadex A-25 column
-
proteins of crude extracts are fractionated using a DEAE-Sephadex A-25 column
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
expression in Escherichia coli
the cSDH sequence is cloned into the pCW and pET28a vector for expression of the protein in Escherichia coli BL21DE3 cells
expressed in Escherichia coli as a His-tagged fusion protein
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
medicine
-
loss of serine deaminase activity results in a hypercolonization phenotype, hypercolonization plays a role in urinary tract infections
analysis
-
online-determination of L-serine concentation in bioreactor
analysis
development of a simple, direct, and continuous assay based on the absorbance of pyruvate, the product of the dehydratase reaction
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Porter, P.N.; Grishaver, M.S.; Jones, O.W.
Characterization of human cystathionine beta-synthase. Evidence for the identity of human L-serine dehydratase and cystathionine beta-synthase
Biochim. Biophys. Acta
364
128-139
1974
Homo sapiens
brenda
Farias, M.E.; Strasser de Saad, A.M.; Pesce de Ruiz Holgado, A.A.; Oliver, G.
Evidence for the presence of L-serine dehydratase in Lactobacillus murinus
J. Gen. Appl. Microbiol.
31
563-567
1985
Ligilactobacillus murinus, Ligilactobacillus murinus CNRZ 313
-
brenda
Newman, E.B.; Kapoor, V.
In vitro studies on L-serine deaminase activity of Escherichia coli K12
Can. J. Biochem.
58
1292-1297
1980
Escherichia coli
brenda
Yeung, Y.G.; Yeung, D.
Comparative studies on threonine and serine dehydratases in rat liver
Int. J. Biochem.
11
161-164
1980
Rattus norvegicus
brenda
Gannon, F.; Bridgeland, E.S.; Jones, K.M.
L-Serine dehydratase from Arthrobacter globiformis
Biochem. J.
161
345-355
1977
Arthrobacter globiformis
brenda
Gannon, F.; Jones, K.M.
An activity stain for L-serine dehydratase in polyacrylamide gels
Anal. Biochem.
79
594-596
1977
Arthrobacter globiformis
brenda
Grillo, M.A.
Serine dehydratase in animal tissues
Acta Vitaminol. Enzymol.
27
51-61
1973
Gallus gallus, Rattus norvegicus
brenda
Morikawa, Y.; Nakamura, N.; Kimura, K.
Purification and some properties of L-serine dehydratase of Corynebacterium sp.
Agric. Biol. Chem.
38
531-537
1974
Corynebacterium sp.
-
brenda
Isenberg, S.; Newman, E.B.
Studies on L-serine deaminase in Escherichia coli K-12
J. Bacteriol.
118
53-58
1974
Escherichia coli
brenda
Simon, D.; Kroeger, H.
Interactions of L-serine dehydratase from rat liver with its coenzyme and substrates
Biochim. Biophys. Acta
334
208-217
1974
Rattus norvegicus
-
brenda
Simon, D.; Hoshino, J.; Kroeger, H.
L-Serine dehydratase from rat liver. Purification and some properties
Biochim. Biophys. Acta
321
361-368
1973
Rattus norvegicus
brenda
Hoshino, J.; Simon, D.; Kroeger, H.
Influence of monovalent cations on the activity of L-serine (L-threonine) dehydratase from rat liver
Eur. J. Biochem.
27
388-394
1972
Rattus norvegicus
brenda
Sagers, R.D.; Carter, J.E.
L-Serine dehydratase (Clostridium acidiurici)
Methods Enzymol.
17B
351-356
1971
Clostridium acidi-urici
-
brenda
Pestana, A.; Sandoval, I.V.; Sols, A.
Inhibition by homocysteine of serine dehydratase and other pyridoxal 5'-phosphate enzymes of the rat through cofactor blockage
Arch. Biochem. Biophys.
146
373-379
1971
Rattus norvegicus
brenda
Kubota, K.; Yokozeki, K.; Ozaki, H.
Effect of L-serine dehydratase activity onL-serine production by Corynebacterium glycinophilum and an examination of the properties of the enzyme
J. Ferment. Bioeng.
67
391-394
1989
Corynebacterium glyciniphilum, Corynebacterium glyciniphilum AJ-3170
-
brenda
Farias, M.E.; Strasser de Saad, A.M.; Pesce de Ruiz Holgado, A.A.; Oliver, G.
Purification and properties of L-serine dehydratase from Lactobacillus fermentum ATCC 14931
Curr. Microbiol.
22
205-211
1991
Limosilactobacillus fermentum
-
brenda
Grabowski, R.; Hofmeister, A.E.M.; Buckel, W.
Bacterial L-serine dehydratases: a new family of enzymes containing iron-sulfur clusters
Trends Biochem. Sci.
18
297-300
1993
Klebsiella aerogenes, Arthrobacter globiformis, Burkholderia cepacia, Clostridium acidi-urici, Escherichia coli, Limosilactobacillus fermentum, Peptoniphilus asaccharolyticus
brenda
Zinecker, H.; Andreesen, J.R.; Pich, A.
Partial purification of an iron-dependent L-serine dehydratase from Clostridium sticklandii
J. Basic Microbiol.
38
147-155
1998
Acetoanaerobium sticklandii
brenda
Hofmeister, A.E.M.; Grabowski, R.; Linder, D.; Buckel, W.
L-Serine and L-threonine dehydratase from Clostridium propionicum. Two enzymes with different prosthetic groups
Eur. J. Biochem.
215
341-349
1993
Anaerotignum propionicum
brenda
Hofmeister, A.E.M.; Albracht, S.P.J.; Buckel, W.
Iron-sulfur cluster-containing L-serine dehydratase from Peptostreptococcus asaccharolyticus: correlation of the cluster type with enzymatic activity
FEBS Lett.
351
416-418
1994
Peptoniphilus asaccharolyticus
brenda
Grabowski, R.; Buckel, W.
Purification and properties of an iron-sulfur containing and pyridoxal-phosphate-independent L-serine dehydratase from Peptostreptococcus asaccharolyticus
Eur. J. Biochem.
199
89-94
1991
Peptoniphilus asaccharolyticus
brenda
Su, H.; Moniakis, J.; Newman, E.B.
Use of gene fusion of the structural gene sdaA to purify L-serine deaminase 1 from Escherichia coli K-12
Eur. J. Biochem.
211
521-527
1993
Escherichia coli
brenda
Newman, E.B.; Walker, C.; Ziegler-Skylakis, K.
A possible mechanism for the in vitro activation of L-serine deaminase activity in Escherichia coli K12
Biochem. Cell Biol.
68
723-728
1990
Escherichia coli
brenda
Hopgood, M.F.; Ballard, F.J.
The relative stability of liver cytosol enzymes incubated in vitro
Biochem. J.
144
371-376
1974
Rattus norvegicus
brenda
Ramos, F.; Wiame, J.M.
Occurrence of a catabolic L-serine (L-threonine) deaminase in Saccharomyces cerevisiae
Eur. J. Biochem.
123
571-576
1982
Saccharomyces cerevisiae
brenda
Suda, M.; Nakagawa, H.
L-Serine dehydratase (rat liver)
Methods Enzymol.
17B
346-351
1971
Rattus norvegicus
-
brenda
Ogawa, H.; Takasugawa, F.; Wakaki, K.; Kishi, H.; Eskandarian, M.R.; Kobayashi, M.; Date, T.; Huh, N.H.; Pitot, H.C.
Rat liver serine dehydratase. Bacterial expression and two folding domains as revealed by limited proteolysis
J. Biol. Chem.
274
12855-12860
1999
Rattus norvegicus
brenda
Sun, L.; Li, X.; Dong, Y.; Yang, M.; Liu, Y.; Han, X.; Zhang, X.; Pang, H.; Rao, Z.
Crystallization and preliminary crystallographic analysis of human serine dehydratase
Acta Crystallogr. Sect. D
59
2297-2299
2003
Homo sapiens
brenda
Yamada, T.; Komoto, J.; Takata, Y.; Ogawa, H.; Pitot, H.C.; Takusagawa, F.
Crystal structure of serine dehydratase from rat liver
Biochemistry
42
12854-12865
2003
Rattus norvegicus (P09367)
brenda
Imai, S.; Kanamoto, R.; Yagi, I.; Kotaru, M.; Saeki, T.; Iwami, K.
Response of the induction of rat liver serine dehydratase to changes in the dietary protein requirement
Biosci. Biotechnol. Biochem.
67
383-387
2003
Rattus norvegicus
brenda
Laroche, M.; Pukall, R.; Ulber, R.
Recovery and characterization of a L-serine dehydratase from the marine bacterium Paracoccus seriniphilus for the construction of bioanalytical systems
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