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Abscess
Enzymatically active Peptostreptococcus magnus: association with site of infection.
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
Enzymic imbalance in serine metabolism in human colon carcinoma and rat sarcoma.
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
Crystal structure of serine dehydratase from rat liver.
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
Periportal expression of the serine dehydratase gene in rat liver.
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.
Leukemia
L-Threonine deaminase as a possible antitumor agent.
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
Enzymes of serine metabolism in normal and neoplastic rat tissues.
Neoplasms
Enzymic imbalance in serine metabolism in human colon carcinoma and rat sarcoma.
Neoplasms
Induction of enzymes by glucagon, glucose repression, adenosine 3',5'-monophosphate concentration during carcinogenesis and in Morris 6918A hepatoma.
Sarcoma
Enzymic imbalance in serine metabolism in human colon carcinoma and rat sarcoma.
Starvation
Amino acid metabolism enzyme activities in the obese Zucker rat.
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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0.49
L-serine O-sulfate
pH 8.0, 37ưC, presence of 1 mM ATP, elimination reaction
130
L-Thr
-
in presence and in absence of 20 mM NH4Cl
additional information
additional information
-
-
-
3.2
D-serine

pH 8.0, 37ưC, presence of 1 mM ATP, elimination reaction
8.5
D-serine
-
wild-type, alpha,beta-elimination, pH 7.4, 37ưC
9
D-serine
-
wild-type, alpha,beta-elimination, presence of ATP, pH 7.4, 37ưC
12
D-serine
-
mutant Q155D, alpha,beta-elimination, presence of ATP, pH 7.4, 37ưC
14.5
D-serine
pH 8.0, 37ưC, presence of 1 mM ATP, racemization reaction
49
D-serine
pH 8.0, 37ưC, racemization reaction
75
D-serine
pH 8.0, 37ưC, elimination reaction
55
D-threonine

-
wild-type, alpha,beta-elimination, presence of ATP, pH 7.4, 37ưC
60
D-threonine
-
mutant Q155D, alpha,beta-elimination, presence of ATP, pH 7.4, 37ưC
0.8
L-Ser

-
-
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
7.8
L-Ser
Clostridium acidi-urici
-
-
17.8
L-Ser
mutant C304A, pH 7.0, temperature not specified in the publication
75
L-Ser
-
in presence of 20 mM NH4Cl
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
2.67
L-serine
-
pH 8.0, 37ưC
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
3.8
L-serine
pH 8.0, 37ưC, presence of 1 mM ATP, racemization reaction
4
L-serine
pH 8.0, 37ưC, presence of 1 mM ATP, elimination reaction
4.3
L-serine
-
pH 7, temperature not specified in the publication
4.7
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme T20A
4.8
L-serine
-
anaerobically isolated enzyme, pH 8.0
5.1
L-serine
-
51ưC, pH 7.6
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
9
L-serine
-
wild-type, alpha,beta-elimination, pH 7.4, 37ưC
10
L-serine
-
wild-type, alpha,beta-elimination, presence of ATP, pH 7.4, 37ưC
10.6
L-serine
-
pH 7, temperature not specified in the publication
11
L-serine
-
mutant Q155D, alpha,beta-elimination, presence of ATP, pH 7.4, 37ưC
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
30
L-serine
pH 8.0, 37ưC, racemization reaction
45
L-serine
-
pH 8.3, 37ưC
50
L-serine
pH 8.3, 37ưC
67
L-serine
-
37ưC, pH 8.3, recombinant SDH
75
L-serine
pH 8.0, 37ưC, elimination reaction
158.8
L-serine
-
effect of chronic acidosis
177
L-serine
-
pH 7.4, 25ưC
182
L-serine
-
pH 7.4, 25ưC, animals treated with thioacetamide for 97 days
189
L-serine
pH 7.0, temperature not specified in the publication, mutant enzyme T446A
0.5
L-threonine

-
-
50
L-threonine
-
37ưC, pH 8.3, recombinant SDH
57
L-threonine
-
pH 8.3, 37ưC
57
L-threonine
pH 8.3, 37ưC
30.7
serine

cSDH L287V
3.1
threonine

cSDH
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2.6
beta-chloro-L-alanine
pH 8.0, 37ưC, presence of 1 mM ATP, elimination reaction
0.49
L-serine O-sulfate
pH 8.0, 37ưC, presence of 1 mM ATP, elimination reaction
31
L-threo-3-hydroxyaspartate
pH 8.0, 37ưC, presence of 1 mM ATP, elimination reaction
0.0033
D-serine

-
wild-type, pH 7.4, 37ưC
0.012
D-serine
-
mutant Q155D, alpha,beta-elimination, presence of ATP, pH 7.4, 37ưC
0.042
D-serine
-
wild-type, alpha,beta-elimination, presence of ATP, pH 7.4, 37ưC
3.2
D-serine
pH 8.0, 37ưC, presence of 1 mM ATP, elimination reaction
14.5
D-serine
pH 8.0, 37ưC, presence of 1 mM ATP, racemization reaction
0.028
D-threonine

-
mutant Q155D, alpha,beta-elimination, presence of ATP, pH 7.4, 37ưC
0.3
D-threonine
-
wild-type, alpha,beta-elimination, presence of ATP, pH 7.4, 37ưC
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
0.033
L-serine

-
mutant Q155D, presence of ATP, pH 7.4, 37ưC
0.033
L-serine
-
wild-type, alpha,beta-elimination, pH 7.4, 37ưC
0.166
L-serine
-
wild-type, alpha,beta-elimination, presence of ATP, pH 7.4, 37ưC
3.8
L-serine
pH 8.0, 37ưC, presence of 1 mM ATP, racemization reaction
4
L-serine
pH 8.0, 37ưC, presence of 1 mM ATP, elimination reaction
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
12
L-serine
-
pH 7, temperature not specified in the publication
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
436
L-serine
-
pH 8.0, 37ưC
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
544
L-serine
-
anaerobically isolated enzyme, pH 8.0
585
L-serine
-
pH 7, temperature not specified in the publication, 500 mM KCl
5.2
L-threonine

-
10.5
L-threonine
pH 8.0, 37ưC, presence of 1 mM ATP, elimination reaction
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10000
-
1 * 26000 + 1 * 10000, enzyme either exists as a heterooctamer or a heterodimer, SDS-PAGE
101700
-
dynamic light scattering
14500
-
1 * 14500 + 1 * 40000, SDS-PAGE
230000
-
gel filtration in absence of Fe2+, octameric enzyme form
27000
-
4 * 27000 + 4 * 30000, SDS-PAGE
33000
2 * 33000, SDS-PAGE, 2 * 34702, calculated
34100
-
determined by SDS-PAGE and immunoblot
34630
hSDH, calculated molecular weight
34670
cSDH, calculated molecular weight
34702
2 * 33000, SDS-PAGE, 2 * 34702, calculated
35000
-
2 * 35000, SDS-PAGE
35000 - 40000
-
gel filtration
35680
His-tagged fusion protein, calculated from cDNA
36121
x * 36121, MALDI-MS, x * 36123, calculated
36123
x * 36121, MALDI-MS, x * 36123, calculated
37000
2 * 37000, SDS-PAGE
45000
x * 45000, calculated
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
49480
-
gel filtration, monomer
51000
-
2 * 51000, His-tagged protein, SDS-PAGE and calculated
51758
-
2 * 51758, electrospray mass spectrometry
52910
-
2 * 52910, calculated for His-tagged protein, 2 * 48460, calculated for native protein, 2 * 46000, SDS-PAGE of His-tagged protein
55000
-
isoforms A and B, gel filtration
64000
-
ultracentrifugation
66810
-
laser light scattering
68000
-
sucrose density gradient centrifugation
72000
Clostridium acidi-urici
-
gel filtration
98950
-
gel filtration, dimer
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
30000
-
4 * 27000 + 4 * 30000, SDS-PAGE
34000

-
2 * 34000, SDS-PAGE
34000
-
2 * 34000, SDS-PAGE, recombinant SDH
40000

-
4 * 40000, SDS-PAGE
40000
-
1 * 14500 + 1 * 40000, 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
57000
gel filtration, dimer
60000

-
gel filtration
66000

-
gel filtration
66000
-
gel filtration, recombinant SDH
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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
cSDH-hSDH
chimeric protein
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
InsP128
cSDH, cSDH lacks a Pro residue corresponding to Pro128 in hSDH
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
DELTA(C458)
mutant enzyme has no detectable activity
DELTA(P456,E457,C458)
mutant enzyme has no detectable activity
E445A
mutant enzyme has no detectable activity
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
H61A
mutant enzyme has no detectable activity
H61N
mutant enzyme has no detectable activity
H61S
mutant enzyme has no detectable activity
K444A
mutant enzyme has no detectable activity
S16A
mutant enzyme has no detectable activity
S17A
kcat/Km for L-serine is 4.8fold lower than the wild-type value
S18A
mutant enzyme has no detectable activity
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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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
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