Information on EC 4.3.1.17 - L-serine ammonia-lyase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
4.3.1.17
-
RECOMMENDED NAME
GeneOntology No.
L-serine ammonia-lyase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-aminoprop-2-enoate = 2-iminopropanoate
show the reaction diagram
(1b), spontaneous
-
-
-
2-iminopropanoate + H2O = pyruvate + NH3
show the reaction diagram
(1c), spontaneous
-
-
-
L-serine = 2-aminoprop-2-enoate + H2O
show the reaction diagram
(1a)
-
-
-
L-serine = pyruvate + NH3
show the reaction diagram
A pyridoxal-phosphate protein.; 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; (overall reaction)
-
-
-
L-serine = pyruvate + NH3
show the reaction diagram
catalytic mechanism
L-serine = pyruvate + NH3
show the reaction diagram
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
show the reaction diagram
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
alpha,beta-position of amino acid; beta-position of amino acid; of NH3, alpha,beta-position of amino acid; of NH3, alpha,beta-position of amino acid, C-N bond cleavage, C-O bond cleavage
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
purine metabolism
-
-
serine metabolism
-
-
Glycine, serine and threonine metabolism
-
-
Cysteine and methionine metabolism
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
Biosynthesis of antibiotics
-
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
bsLSD type 1
-
-
cSDH
cancerous SDH
Dehydratase, L-serine
-
-
-
-
EC 4.2.1.13
-
-
formerly
-
GSU0486
Geobacter sulfurreducens DL-1, Geobacter sulfurreducens DL1
-
-
-
HSDH
hepatic SDH
L-Hydroxy amino acid dehydratase
-
-
-
-
L-SD
-
-
-
-
L-SD1
-
-
-
-
L-SD2
-
-
-
-
L-serine ammonia-lyase
-
L-serine ammonia-lyase
-
-
L-serine ammonia-lyase
-
L-Serine deaminase
-
-
-
-
L-Serine deaminase
-
-
L-Serine deaminase
-
-
-
L-Serine deaminase
-
-
L-Serine deaminase
Penicillium palitans NRC-510
-
-
-
L-serine deaminase 2
-
L-serine dehydratase
-
-
L-serine dehydratase
-
-
-
L-serine dehydratase
-
-
L-serine dehydratase
-
L-serine dehydratase
-
-
L-serine dehydratase
-
L-serine dehydratase
-
-
L-serine dehydratase
Penicillium palitans NRC-510
-
-
-
L-serine dehydratase
-
L-serine dehydratase 1
-
L-serine dehydratase 2
-
L-threonine deaminase
-
-
L-threonine deaminase
-
-
-
L-threonine deaminase
-
-
L-threonine deaminase
Penicillium palitans NRC-510
-
-
-
L-threonine dehydratase
-
-
L-threonine dehydratase
-
-
-
L-threonine dehydratase
-
-
L-threonine dehydratase
-
L-threonine dehydratase
-
-
L-threonine dehydratase
Penicillium palitans NRC-510
-
-
-
SD
-
-
-
-
SdaA
gene name
SdaB
gene name
SDH
-
-
-
-
SDH-like-1
-
Serine deaminase
-
-
-
-
Serine deaminase
-
-
Serine dehydratase
-
-
-
-
Serine dehydratase
-
Serine dehydratase
-
-
Serine dehydratase
-
serine dehydratase like-1
-
tdcB
Geobacter sulfurreducens DL-1, Geobacter sulfurreducens DL1
-
-
-
TdcG
gene name
additional information
-
L-serine dehydratase and cystathionine beta-synthase are the same enzyme
CAS REGISTRY NUMBER
COMMENTARY
9014-27-1
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Clostridium acidi-urici
-
-
-
Manually annotated by BRENDA team
Corynebacterium glycinophilum
strain AJ-3170 and various mutants
-
-
Manually annotated by BRENDA team
Corynebacterium glycinophilum AJ-3170
strain AJ-3170 and various mutants
-
-
Manually annotated by BRENDA team
anaerobically inducible enzyme
-
-
Manually annotated by BRENDA team
three genes sdaA, sdaB, tdcG encoding the isozymes of SDH
-
-
Manually annotated by BRENDA team
Escherichia coli K12
K12
-
-
Manually annotated by BRENDA team
strain DL-1, ATCC 51573, gene GSU0486 or tcdB
-
-
Manually annotated by BRENDA team
Geobacter sulfurreducens DL-1
strain DL-1, ATCC 51573, gene GSU0486 or tcdB
-
-
Manually annotated by BRENDA team
bifunctional enzyme, racemization of serine and elimination of L-serine and L-serine-O-sulfate to form pyruvate
-
-
Manually annotated by BRENDA team
strain CNRZ 313
-
-
Manually annotated by BRENDA team
Lactobacillus murinus CNRZ 313
strain CNRZ 313
-
-
Manually annotated by BRENDA team
type 2 enzyme
UniProt
Manually annotated by BRENDA team
bifunctional enzyme, racemization of serine and elimination of L-serine and L-serine-O-sulfate to form pyruvate
Swissprot
Manually annotated by BRENDA team
bifunctional enzymes, racemization of serine and alpha,beta-elimination of L-serine
-
-
Manually annotated by BRENDA team
isoforms A and B, bifunctional enzymes, racemization of serine and elimination of L-serine and L-serine-O-sulfate to form pyruvate
-
-
Manually annotated by BRENDA team
Penicillium palitans NRC-510
NRC-510
-
-
Manually annotated by BRENDA team
aged 3 to 15 weeks, fed on a 25% casein diet for one week
-
-
Manually annotated by BRENDA team
includes 4.3.1.17 and 4.3.1.19; male Sprague-Dawley rat
UniProt
Manually annotated by BRENDA team
isoenzyme I and II
-
-
Manually annotated by BRENDA team
male wistar rat
-
-
Manually annotated by BRENDA team
multiple forms
-
-
Manually annotated by BRENDA team
SDH activity and its gene expression are induced in both growing and mature rats when their protein intake exceeds their nutrintional requirements
-
-
Manually annotated by BRENDA team
treated by oral intake of thioacetamide
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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; 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; 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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-chloro-L-alanine
3-chloropropenoic acid + NH3
show the reaction diagram
-
-
?
D-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
D-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
D-serine
pyruvate + NH3
show the reaction diagram
-
alpha,beta-elimination reaction
-
?
D-serine
pyruvate + NH3
show the reaction diagram
elimination reaction
-
?
D-serine
L-serine
show the reaction diagram
racemization reaction
-
r
D-serine
L-serine
show the reaction diagram
-
racemization reaction
-
r
D-serine
L-serine
show the reaction diagram
-
racemization reaction
-
r
L-allo-threonine
2-oxobutyrate + NH3
show the reaction diagram
-
at 4.6% of the rate with L-serine
-
?
L-Leu
3-Hydroxy-2-oxopropionate + NH3
show the reaction diagram
Corynebacterium glycinophilum, Corynebacterium glycinophilum AJ-3170
-
3% of the activity with L-Ser
-
-
L-Ser
?
show the reaction diagram
-
the metabolic role may be related to serine toxicity
-
-
-
L-Ser
?
show the reaction diagram
-
constitutive enzyme, repressed by glucose
-
-
-
L-Ser
?
show the reaction diagram
Escherichia coli K12
-
the metabolic role may be related to serine toxicity
-
-
-
L-Ser
?
show the reaction diagram
Lactobacillus murinus CNRZ 313
-
constitutive enzyme, repressed by glucose
-
-
-
L-Ser
pyruvate + NH3
show the reaction diagram
-
-
ir
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
Clostridium acidi-urici
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
Clostridium acidi-urici, Peptoniphilus asaccharolyticus
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
ir
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
alpha,beta-elimination
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
specific for L-Ser
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
specific for L-Ser
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
specific for L-Ser
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
specific for L-Ser
-
-
L-serine
pyruvate + NH3
show the reaction diagram
Corynebacterium glycinophilum
-
specific for L-Ser
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
alpha,beta-elimination reaction
-
?
L-serine
pyruvate + NH3
show the reaction diagram
elimination reaction
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
elimination reaction
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
elimination reaction
-
?
L-serine
pyruvate + NH3
show the reaction diagram
SDH is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes dehydration of L-Ser/Thr to yield pyruvate/ketobutyrate and ammonia, a rigid pyridine ring pocket is necessary for cSDH having a flexible substrate binding-loop
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
wild-type enzyme shows almost no activity with D-serine
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
Geobacter sulfurreducens DL1, Geobacter sulfurreducens DL-1
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
Penicillium palitans NRC-510
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
Corynebacterium glycinophilum AJ-3170
-
specific for L-Ser
-
-
L-serine
pyruvate + NH3
show the reaction diagram
Escherichia coli K12
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
Escherichia coli K12
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
Escherichia coli K12
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
Escherichia coli K12
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
Lactobacillus murinus CNRZ 313
-
specific for L-Ser
-
-
L-serine
D-serine
show the reaction diagram
racemization reaction
-
r
L-serine
D-serine
show the reaction diagram
-
racemization reaction
-
r
L-serine
D-serine
show the reaction diagram
-
racemization reaction
-
r
L-serine
D-serine
show the reaction diagram
-
reacemization reaction
-
r
L-serine
D-serine
show the reaction diagram
-
recemization reaction
-
r
L-serine O-sulfate
O-sulfopyruvate + NH3
show the reaction diagram
elimination reaction
-
?
L-serine-O-sulfate
? + NH3
show the reaction diagram
-
elimination reaction
-
?
L-serine-O-sulfate
O-sulfopyruvate + NH3
show the reaction diagram
-
elimination reaction
-
?
L-Thr
3-Hydroxy-2-oxobutyrate + NH3
show the reaction diagram
-
-
-
-
L-Thr
3-Hydroxy-2-oxobutyrate + NH3
show the reaction diagram
Corynebacterium glycinophilum
-
1% of the activity with L-Ser
-
-
L-Thr
3-Hydroxy-2-oxobutyrate + NH3
show the reaction diagram
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
-
?
L-Thr
3-Hydroxy-2-oxobutyrate + NH3
show the reaction diagram
Corynebacterium glycinophilum AJ-3170
-
1% of the activity with L-Ser
-
-
L-threo-3-hydroxyaspartate
oxaloacetate + NH3
show the reaction diagram
-
-
?
L-threonine
2-oxo-butanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutyrate + NH3
show the reaction diagram
-
-
?
L-threonine
2-oxobutyrate + NH3
show the reaction diagram
-
-
?
L-threonine
2-oxobutyrate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutyrate + NH3
show the reaction diagram
-
-
?
L-threonine
2-oxobutyrate + NH3
show the reaction diagram
-
at 2.7% of the rate with L-serine
-
?
L-threonine
3-hydroxy-2-butenoic acid + NH3
show the reaction diagram
-
alpha,beta-elimination reaction
-
?
L-threonine
alpha-ketobutyrate + NH3
show the reaction diagram
-
-
-
?
L-threonine
alpha-ketobutyrate + NH3
show the reaction diagram
-
-
-
?
L-threonine
alpha-ketobutyrate + NH3
show the reaction diagram
-
-
-
?
L-threonine
alpha-ketobutyrate + NH3
show the reaction diagram
-
-
-
?
L-threonine
alpha-ketobutyrate + NH3
show the reaction diagram
-
-
-
?
L-threonine
alpha-ketobutyrate + NH3
show the reaction diagram
Penicillium palitans NRC-510
-
-
-
?
L-Trp
?
show the reaction diagram
Corynebacterium glycinophilum, Corynebacterium glycinophilum AJ-3170
-
17% of the activity with L-Ser
-
-
-
additional information
?
-
-
no substrate: L-threonine
-
-
-
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
?
-
-
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
?
-
enzyme shows homotopic cooperativity, Hill coefficient of wild-type is 1.7
-
-
-
additional information
?
-
cytotoxic early protein 77 of mycobacteriophage L5 interacts with MSMEG_3532
-
-
-
additional information
?
-
Geobacter sulfurreducens DL1, Geobacter sulfurreducens DL-1
-
GSU0486 mainly catalyzes the deamination of L-threonine, EC 4.3.1.19
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-Ser
?
show the reaction diagram
-
the metabolic role may be related to serine toxicity
-
-
-
L-Ser
?
show the reaction diagram
-
constitutive enzyme, repressed by glucose
-
-
-
L-Ser
?
show the reaction diagram
Escherichia coli K12
-
the metabolic role may be related to serine toxicity
-
-
-
L-Ser
?
show the reaction diagram
Lactobacillus murinus CNRZ 313
-
constitutive enzyme, repressed by glucose
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
P09367
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
ir
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
P09367
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
Q96GA7
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
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
Geobacter sulfurreducens DL1, Geobacter sulfurreducens DL-1
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
Penicillium palitans NRC-510
-
-
-
?
L-threonine
alpha-ketobutyrate + NH3
show the reaction diagram
-
-
-
?
L-threonine
alpha-ketobutyrate + NH3
show the reaction diagram
-
-
-
?
L-threonine
alpha-ketobutyrate + NH3
show the reaction diagram
-
-
-
?
L-threonine
alpha-ketobutyrate + NH3
show the reaction diagram
Penicillium palitans NRC-510
-
-
-
?
additional information
?
-
A0QY48
cytotoxic early protein 77 of mycobacteriophage L5 interacts with MSMEG_3532
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
required, maximal activity at 0.34 mM
pyridoxal 5'-phosphate
-
Km: 0.0003 mM; one mol of enzyme contains two mol of pyridoxal phosphate
pyridoxal 5'-phosphate
-
coenzyme; 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
-
coenzyme
pyridoxal 5'-phosphate
-
prosthetic group; 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-independent enzyme
pyridoxal 5'-phosphate
-
pyridoxal-5'-phosphate-independent enzyme
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
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
-
dependent on
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
additional information
-
not dependent on pyridoxal 5'-phosphate
-
additional information
-
pyridoxal 5'-phosphate independent
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
-
Ca2+
-
may partially replace Mg2+
Fe2+
Clostridium acidi-urici
-
Km: 0.1 mM; required
Fe2+
Corynebacterium glycinophilum
-
slight activation by FeCl2
Fe2+
-
Km: 0.55 mM; required
Fe2+
Clostridium acidi-urici
-
required
Fe2+
-
requires activation
Fe2+
-
required for activity, Fe-S cluster
Fe2+
-
iron-sulfur enzyme
Iron
-
enzyme contains one [4Fe-4S]cluster per heterodimer
Iron
-
iron-sulfur-dependent enzyme
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
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
K+
-
slight stimulation
K+
-
stimulating
K+
-
required, addition results in strong activation
K+
addition results in weak activation
KCl
-
nonspecific requirement for a monovalent or bivalent cation. Half-maximal activity is produced with 22.5 mM KCl
Mg2+
-
required, both activities
Mg2+
-
required by both isoforms A and B
MgCl2
-
nonspecific requirement for a monovalent or bivalent cation. Half-maximal activity with 1.0 mM MgCl2
MgCl2
-
activates
Mn2+
-
increases activity
Mn2+
-
-
Mn2+
-
may partially replace Mg2+
NH4+
-
slight stimulation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
no effect
2-oxobutyrate
20 mM: 49.3% inhibition, not reversed by 5 mM AMP
AlK(SO4)2
-
-
ammonia
product inhibition, noncompetitive
ATP
-
inhibitory to L-serine O-sulfate dehydration reaction, activating for racemization reraction
Co2+
-
inhibition of both activities
Co2+
-
inhibition
Cu2+
-
inhibition of both activities
CuCl2
-
0.7 mM, 50% inhibition
D-Ser
-
competitive
D-Ser
-
competitive
D-serine
-
100 mM, 40% inhibition
D-serine
-
competitive
D-serine
competitive
EDTA
-
inhibition of both activities
ethanolamine
-
-
Fe2+
-
slight inhibition of both activities
Gly
Corynebacterium glycinophilum
-
-
glyoxylate
20 mM: 54.1% inhibition, not reversed by 5 mM AMP
homocysteine
-
noncompetitive with respect to substrate, competitive with regard to pyridoxal 5'-phosphate
hydroxylamine
-
-
imidazole
-
-
L-alanine
-
-
L-Cys
-
competitive
L-Cys
Corynebacterium glycinophilum
-
-
L-cysteine
-
50 mM, 95% inhibition
L-cysteine
-
competitive
L-cysteine
competitive
L-cysteine
competitive
L-Thr
-
competitive
L-threonine
-
100 mM, 56% inhibition
L-Trp
Corynebacterium glycinophilum
-
-
L-Val
Corynebacterium glycinophilum
-
-
NH4Cl
-
significant fall in the serine-dehydratase expression during experimental chronic acidosis, acidosis is induced by ingestion of 0.28 M ammonium chloride solution
Ni2+
-
slight inhibition of both activities
Ni2+
-
inhibition
oxygen
-
bsLSD is highly sensitive to oxygen
oxygen
lpLSD is weakly sensitive to oxygen
PCMB
-
NH4+ protects
pyruvate
-
competitive
pyruvate
20 mM: 45.3% inhibition, not reversed by 5 mM AMP
pyruvate
product inhibition, competitive
Zn2+
-
inhibition of both activities
MnCl2
Corynebacterium glycinophilum
-
-
additional information
-
NaBH4 has no effect
-
additional information
-
not inhibitory: L-alanine
-
additional information
-
TcdB is not inhibited by isoleucine
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
sulfhydryl reagents
Clostridium acidi-urici
-
required
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.2
D-serine
-
pH 8.0, 37C, presence of 1 mM ATP, elimination reaction
8.5
D-serine
-
wild-type, alpha,beta-elimination, pH 7.4, 37C
9
D-serine
-
wild-type, alpha,beta-elimination, presence of ATP, pH 7.4, 37C
12
D-serine
-
mutant Q155D, alpha,beta-elimination, presence of ATP, pH 7.4, 37C
14.5
D-serine
-
pH 8.0, 37C, presence of 1 mM ATP, racemization reaction
49
D-serine
-
pH 8.0, 37C, racemization reaction
75
D-serine
-
pH 8.0, 37C, elimination reaction
55
D-threonine
-
wild-type, alpha,beta-elimination, presence of ATP, pH 7.4, 37C
60
D-threonine
-
mutant Q155D, alpha,beta-elimination, presence of ATP, pH 7.4, 37C
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
-
-
8.33
L-Ser
-
-
17.8
L-Ser
mutant C304A, pH 7.0, temperature not specified in the publication
70
L-Ser
-
-
75
L-Ser
-
in presence of 20 mM NH4Cl
100
L-Ser
-
without NH4+
420
L-Ser
-
-
0.00258
L-serine
pH 7, temperature not specified in the publication, Vmax: 11.7/min/mg
0.27
L-serine
-
-
2.67
L-serine
-
pH 8.0, 37C
3.8
L-serine
-
pH 8.0, 37C, presence of 1 mM ATP, racemization reaction
4
L-serine
-
pH 8.0, 37C, presence of 1 mM ATP, elimination reaction
4.3
L-serine
-
pH 7, temperature not specified in the publication
4.8
L-serine
-
anaerobically isolated enzyme, pH 8.0
5.1
L-serine
-
51C, pH 7.6
5.1
L-serine
pH 7, temperature not specified in the publication
9
L-serine
-
wild-type, alpha,beta-elimination, pH 7.4, 37C
10
L-serine
-
wild-type, alpha,beta-elimination, presence of ATP, pH 7.4, 37C
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, 37C
13.6
L-serine
-
pH 7, temperature not specified in the publication, 100 mM KCl
14.6
L-serine
-
-
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, 37C, racemization reaction
45
L-serine
-
pH 8.3, 37C
50
L-serine
-
pH 8.3, 37C
67
L-serine
-
37C, pH 8.3, recombinant SDH
75
L-serine
-
pH 8.0, 37C, elimination reaction
123.3
L-serine
-
control
158.8
L-serine
-
effect of chronic acidosis
177
L-serine
-
pH 7.4, 25C
182
L-serine
-
pH 7.4, 25C, animals treated with thioacetamide for 97 days
0.49
L-serine O-sulfate
-
pH 8.0, 37C, presence of 1 mM ATP, elimination reaction
130
L-Thr
-
in presence and in absence of 20 mM NH4Cl
0.5
L-threonine
-
-
7.3
L-threonine
-
50
L-threonine
-
37C, pH 8.3, recombinant SDH
30.7
serine
-
cSDH L287V
32.2
serine
-
cSDH
34.5
serine
-
cSDH +Pro
35.7
serine
-
hSDH -Pro
44.4
serine
-
cSDH-hSDH
67.3
serine
-
hSDH
3.1
threonine
-
cSDH
3.5
threonine
-
cSDH +Pro
4.2
threonine
-
cSDH L287V
13.2
threonine
-
cSDH-hSDH
14.9
threonine
-
hSDH -Pro
59.5
threonine
-
hSDH
57
L-threonine
-
pH 8.3, 37C
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.6
beta-chloro-L-alanine
Mus musculus
-
pH 8.0, 37C, presence of 1 mM ATP, elimination reaction
0.0033
D-serine
Mus musculus
-
wild-type, pH 7.4, 37C
0.012
D-serine
Mus musculus
-
mutant Q155D, alpha,beta-elimination, presence of ATP, pH 7.4, 37C
0.042
D-serine
Mus musculus
-
wild-type, alpha,beta-elimination, presence of ATP, pH 7.4, 37C
3.2
D-serine
Mus musculus
-
pH 8.0, 37C, presence of 1 mM ATP, elimination reaction
14.5
D-serine
Mus musculus
-
pH 8.0, 37C, presence of 1 mM ATP, racemization reaction
0.028
D-threonine
Mus musculus
-
mutant Q155D, alpha,beta-elimination, presence of ATP, pH 7.4, 37C
0.3
D-threonine
Mus musculus
-
wild-type, alpha,beta-elimination, presence of ATP, pH 7.4, 37C
323
L-Ser
Legionella pneumophila
Q5ZXE1
mutant C304A, pH 7.0, temperature not specified in the publication
330
L-Ser
Legionella pneumophila
Q5ZXE1
wild-type, pH 7.0, temperature not specified in the publication
359
L-Ser
Legionella pneumophila
Q5ZXE1
mutant C221A, pH 7.0, temperature not specified in the publication
467
L-Ser
Legionella pneumophila
Q5ZXE1
mutant C226A, pH 7.0, temperature not specified in the publication
506
L-Ser
Legionella pneumophila
Q5ZXE1
mutant C183A, pH 7.0, temperature not specified in the publication
512
L-Ser
Legionella pneumophila
Q5ZXE1
mutant C458A, pH 7.0, temperature not specified in the publication
0.033
L-serine
Mus musculus
-
mutant Q155D, presence of ATP, pH 7.4, 37C; wild-type, alpha,beta-elimination, pH 7.4, 37C
0.166
L-serine
Mus musculus
-
wild-type, alpha,beta-elimination, presence of ATP, pH 7.4, 37C
3
L-serine
Entamoeba histolytica
B1N2N4
-
3.8
L-serine
Mus musculus
-
pH 8.0, 37C, presence of 1 mM ATP, racemization reaction
4
L-serine
Mus musculus
-
pH 8.0, 37C, presence of 1 mM ATP, elimination reaction
12
L-serine
Bacillus subtilis
-
pH 7, temperature not specified in the publication
184
L-serine
Bacillus subtilis
-
pH 7, temperature not specified in the publication, 100 mM KCl
286
L-serine
Legionella pneumophila
Q5ZXE1
pH 7, temperature not specified in the publication
436
L-serine
Escherichia coli
-
pH 8.0, 37C
465
L-serine
Bacillus subtilis
-
pH 7, temperature not specified in the publication, 300 mM KCl
544
L-serine
Escherichia coli
-
anaerobically isolated enzyme, pH 8.0
585
L-serine
Bacillus subtilis
-
pH 7, temperature not specified in the publication, 500 mM KCl
0.49
L-serine O-sulfate
Mus musculus
-
pH 8.0, 37C, presence of 1 mM ATP, elimination reaction
31
L-threo-3-hydroxyaspartate
Mus musculus
-
pH 8.0, 37C, presence of 1 mM ATP, elimination reaction
5.2
L-threonine
Entamoeba histolytica
B1N2N4
-
10.5
L-threonine
Mus musculus
-
pH 8.0, 37C, presence of 1 mM ATP, elimination reaction
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
18
L-Ser
Legionella pneumophila
Q5ZXE1
mutant C304A, pH 7.0, temperature not specified in the publication
262
74
L-Ser
Legionella pneumophila
Q5ZXE1
mutant C458A, pH 7.0, temperature not specified in the publication
262
120
L-Ser
Legionella pneumophila
Q5ZXE1
mutant C221A, pH 7.0, temperature not specified in the publication
262
170
L-Ser
Legionella pneumophila
Q5ZXE1
mutant C226A, pH 7.0, temperature not specified in the publication; wild-type, pH 7.0, temperature not specified in the publication
262
230
L-Ser
Legionella pneumophila
Q5ZXE1
mutant C183A, pH 7.0, temperature not specified in the publication
262
0.2
L-serine
Entamoeba histolytica
B1N2N4
-
95
1
L-serine
Bacillus subtilis
-
pH 7, temperature not specified in the publication
95
14
L-serine
Bacillus subtilis
-
pH 7, temperature not specified in the publication, 100 mM KCl
95
18
L-serine
Bacillus subtilis
-
pH 7, temperature not specified in the publication, 300 mM KCl
95
20
L-serine
Bacillus subtilis
-
pH 7, temperature not specified in the publication, 500 mM KCl
95
57
L-serine
Legionella pneumophila
Q5ZXE1
pH 7, temperature not specified in the publication
95
0.7
L-threonine
Entamoeba histolytica
B1N2N4
-
250
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.7
CuCl2
-
-
1.41
D-serine
-
pH 8.0, 37C
10
D-serine
pH 7.0, temperature not specified in the publication
0.9
L-alanine
-
pH 8.0, 37C
0.1
L-cysteine
pH 7.0, temperature not specified in the publication
1.1
L-cysteine
substrate L-serine
2.2
L-cysteine
substrate L-threonine
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10
ATP
Entamoeba histolytica
B1N2N4
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0006
kidney, diet 10% casein; kidney, diet Leu
0.0008
kidney, diet 20% casein; kidney, diet Ile; kidney, diet Val
0.01775
-
effect of chronic acidosis
0.034
liver, diet Ile
0.0365
liver, diet 10% casein
0.041
-
strain DL-1
0.0416
liver, diet Val
0.04264
-
control
0.1262
liver, diet 20% casein
0.1419
liver, diet Leu
0.262
Corynebacterium glycinophilum
-
-
96
-
substrate L-threonine, pH 8.3, 37C
115
-
recombinant SdaA
116
-
substrate L-threonine, pH 8.3, 37C
137
-
substrate L-serine, pH 8.3, 37C
174.2
-
isoenzyme II
200
-
substrate L-serine, pH 8.3, 37C
226.9
-
isoenzyme I
307
-
anaerobically isolated enzyme, pH 8.0
additional information
-
activity stain in polyacrylamide gels
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
-
negligible activity below
6.5 - 9.5
-
pH 6.5: about 40% of maximal activity, pH 9.5: about 90% of maximal activity
7 - 9.5
Corynebacterium glycinophilum
-
pH 7: about 35% of maximal activity, pH 9.5: about 35% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
activity assay
37
-
activity assay
37
-
activity assay
37
-
assay at
40
Corynebacterium glycinophilum
-
-
50
-
activity assay
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18 - 50
Corynebacterium glycinophilum
-
18C: about 50% of maximal activity, 50C: about 25% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
cancerous SDH
Manually annotated by BRENDA team
cancer cell line-specific isozyme cSDH
Manually annotated by BRENDA team
-
cancerous SDH
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
predominantly localized in perivenous region
Manually annotated by BRENDA team
-
confined to periportal region
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
cancerous SDH
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Lactobacillus murinus CNRZ 313
-
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30500
-
gel filtration
651527
34100
-
determined by SDS-PAGE and immunoblot
677454
34630
-
hSDH, calculated molecular weight
678411
34670
-
cSDH, calculated molecular weight
678411
35000 - 40000
-
gel filtration
651527
35680
His-tagged fusion protein, calculated from cDNA
729942
49480
-
gel filtration, monomer
729219
53000
-
gel filtration
650851
55000
-
isoforms A and B, gel filtration
662950
57000
-
gel filtration in presence of 10 mM Fe2+, dimeric enzyme form
210792
57000
gel filtration, dimer
729942
60000
-
gel filtration
210784
60000
-
gel filtration
665219
63500
-
-
210780
64000
-
ultracentrifugation
651527
66000
-
gel filtration
210800
66000
-
gel filtration, recombinant SDH
651919
66810
-
laser light scattering
651527
68000
-
sucrose density gradient centrifugation
210784
72000
Clostridium acidi-urici
-
gel filtration
210786
78000
-
gel filtration
661725
98950
-
gel filtration, dimer
729219
101700
-
dynamic light scattering
664943
107000
-
gel filtration
665546
123000
-
gel filtration
651494
130000
Corynebacterium glycinophilum
-
gel filtration
210788
150000
-
gel filtration
210789
180000
-
gradient PAGE
210794
200000
-
gel filtration
210794
230000
-
gel filtration in absence of Fe2+, octameric enzyme form
210792
250000
-
gel filtration
210791
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 36121, MALDI-MS, x * 36123, calculated
?
x * 45000, calculated
dimer
-
2 * 34000
dimer
-
2 * 35000, SDS-PAGE
dimer
-
1 * 25000 + 1 * 30000, the enzyme is composed of two different subunits in a 1:1 stoichiometry, forming heterodimers to heterooctamers
dimer
-
1 * 26000 + 1 * 10000, enzyme either exists as a heterooctamer or a heterodimer, SDS-PAGE
dimer
-
1 * 14500 + 1 * 40000, SDS-PAGE
dimer
-
2 * 51758, electrospray mass spectrometry
dimer
-
2 * 34000, SDS-PAGE
dimer
-
2 * 34000, SDS-PAGE, recombinant SDH
dimer
-
2 * 37000, 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
-
2 * 33000, SDS-PAGE, 2 * 34702, calculated
dimer
-
2 * 51000, His-tagged protein, SDS-PAGE and calculated
dimer
-
gel filtration, 2 * 49476, only dimer displays catalytic activity. In the absence of substrate, lpLSD is predominately a dimer
hexamer
-
3 * 25000 + 3 * 30000, the enzyme is composed of two different subunits in a 1:1 stoichiometry, forming heterodimers to heterooctamers
monomer
-
1 *30500, SDS-PAGE, immunoblot
octamer
-
4 * 25000 + 4 * 30000, the enzyme is composed of two different subunits in a 1:1 stoichiometry, forming heterodimers to heterooctamers
octamer
-
4 * 27000 + 4 * 30000, SDS-PAGE
octamer
-
4 * 26000 + 4 * 30000, enzyme either exists as a heterooctamer or a heterodimer, SDS-PAGE
tetramer
-
4 * 40000, SDS-PAGE
tetramer
-
2 * 25000 + 2 * 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
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
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 21C, 1 week, X-ray diffraction structure determination and analysis at 2.8 A resolution
structure of A65S hSDH mutant is determined at 1.3 A resolution
-
crystal structures of apo-SDH and holo-SDH, crystallized with O-methylserine, at 2.8 A and 2.6 A resolution, respectively
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
-
37C, 30 min, about 50% loss of activity
210781
5.5
-
37C, 30 min, about 40% loss of activity
210781
6 - 7
-
37C, 30 min, about 25% loss of activity
210781
8
-
37C, 30 min, about 45% loss of activity
210781
8.5
-
37C, 30 min, 50% loss of activity
210781
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0
-
30 min, 45% loss of activity
210775
30
-
pH 6.2, 30 min, stable up to
210781
37
-
complete loss of activity within 30 min. Fe2+, L-Ser D-Ser or ethanolamine decrease the loss of activity at 37C
210775
40
-
pH 6.2, 30 min, about 50% loss of activity
210781
45
-
10 min, 70% loss of activity
210774
45
-
10 min, stable up to
5592
50
-
about 90% loss of activity
210781
50
-
10 min, about 10% loss of activity
5592
55
-
10 min, complete loss of activity
210774
55
-
complete loss of activity after 4 min. NH4Cl, KCl or (NH4)2SO4 stabilize
210785
55
-
10 min, about 50% loss of activity
5592
60
-
10 min, about 75% loss of activity
5592
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
extreme instability does not permit purification to homogeneity
-
L-Cys and D-Ser stabilize enzyme activity
-
it is absolutely critical that dilutions of the purified enzyme be made in buffer containing 50% glycerol, otherwise the enzyme rapidly loses activity
-
unstable in all attempts at purification
-
suszeptible to proteases e.g. trypsin
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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+
-
210792
inactivated upon exposure to air, reactivated by Fe2+ under aerobic conditions
-
210791
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
-
210790
rapid loss of activity upon exposure to air, reactivation by Fe2+
-
210794
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, pH 7.0-8.0, stable over many months, enzyme in crude extract
-
-70C, 0.6 mg/ml protein, 30% loss of activity after 1 month, purified enzyme
-
-20C, 40% loss of activity after 24 h, 0.76 mg/ml protein concentration, partially purified enzyme
Corynebacterium glycinophilum
-
4C, 90% loss of activity after 24 h, 0.76 mg/ml protein concentration, partially purified enzyme
Corynebacterium glycinophilum
-
-10C, 40% glycerol, loss of activity within 1 week
-
0C, 45% loss of activity after 30 min
-
unstable within the cell in the presence of its inducers, Gly and Leu, but not in their absence
-
-80C, stable for more than 2 weeks
-
0C, stable for at least 2 weeks
-
-80C, at least 1 month, no loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
proteins of crude extracts are fractionated using a DEAE-Sephadex A-25 column
-
using cobalt-based affinity columns
-
recombinant His-tagged SdaA
-
-
Clostridium acidi-urici
-
strain AJ-3170
Corynebacterium glycinophilum
-
immobilized metal ion affinity chromatography (Ni2+)
anaerobic purification of His-tagged enzyme, purified protein is brown in colour
-
recombinant protein, purification under anaerobic conditions
-
use of gene fusion of the structural gene sdaA to purify L-serine deaminase 1
-
cSDH is purified using a Sephacryl S-200 and a Ni2+-NAT column
-
expression in Escherichia coli with N-terminal His-tag, purification protocol from inclusion bodies
-
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
-
using Ni-NTA chromatography
-
using cobalt-based affinity columns
using cobalt-based Talon immobilized metal affinity columns
-
both isoforms A and B
-
recombinant enzyme expressed in insect cells
-
using Ni-NTA chromatography
partially purified
-
proteins of crude extracts are fractionated using a DEAE-Sephadex A-25 column
-
recombinant protein expressed in Escherichia coli
-
recombinant SDH
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
-
expression in Escherichia coli
-
His-tagged version expressed in Escherichia coli BL21(DE3)
gene tcdB, phylogenetic analysis of threonine ammonia-lyases
-
cancer cell isozyme cSDH, expression in Escherichia coli strain BL21
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
-
expressed in Escherichia coli as a His-tagged fusion protein
expression in Escherichia coli
-
ENGINEERING
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
cSDH-hSDH
-
chimeric protein
DELTAP128
-
hSDH
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
L287V
-
cSDH
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
44% of wild-type activity. Enzyme retains the positive cooperativity seen in the native enzyme
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
loss of serine deaminase activity results in a hypercolonization phenotype, hypercolonization plays a role in urinary tract infections
analysis
development of a simple, direct, and continuous assay based on the absorbance of pyruvate, the product of the dehydratase reaction
analysis
-
online-determination of L-serine concentation in bioreactor