Information on EC 6.2.1.5 - Succinate-CoA ligase (ADP-forming)

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

EC NUMBER
COMMENTARY hide
6.2.1.5
-
RECOMMENDED NAME
GeneOntology No.
Succinate-CoA ligase (ADP-forming)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + succinate + CoA = ADP + phosphate + succinyl-CoA
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
anaerobic energy metabolism (invertebrates, mitochondrial)
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
C5-Branched dibasic acid metabolism
-
-
Carbon fixation pathways in prokaryotes
-
-
Citrate cycle (TCA cycle)
-
-
citric acid cycle
-
-
incomplete reductive TCA cycle
-
-
Metabolic pathways
-
-
methylaspartate cycle
-
-
Microbial metabolism in diverse environments
-
-
partial TCA cycle (obligate autotrophs)
-
-
Propanoate metabolism
-
-
pyruvate fermentation to acetate V
-
-
pyruvate fermentation to acetate VI
-
-
reductive TCA cycle I
-
-
reductive TCA cycle II
-
-
TCA cycle I (prokaryotic)
-
-
TCA cycle II (plants and fungi)
-
-
TCA cycle III (animals)
-
-
TCA cycle V (2-oxoglutarate:ferredoxin oxidoreductase)
-
-
SYSTEMATIC NAME
IUBMB Comments
Succinate:CoA ligase (ADP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9080-33-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strains 1023 and DSM 2002, aarABC region, gene aarC
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
human isolate, strain DMP/02-328, ATCC 50177
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
blowfly
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene CG11963
-
-
Manually annotated by BRENDA team
K12
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
soybean
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain ATCC 25978
-
-
Manually annotated by BRENDA team
Pigeon
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
B1Y9F9: subunit beta, B1Y9G0: subunit alpha
B1Y9F9 and B1Y9G0
UniProt
Manually annotated by BRENDA team
B1Y9F9: subunit beta, B1Y9G0: subunit alpha
B1Y9F9 and B1Y9G0
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain DSM639
-
-
Manually annotated by BRENDA team
strain DSM639
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain KOD1
-
-
Manually annotated by BRENDA team
strain AT-62
-
-
Manually annotated by BRENDA team
strain AT-62
-
-
Manually annotated by BRENDA team
gene scsB
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
additional information
organisms with a very high Km-value for ADP and a low Km value for GDP are listed at EC 6.2.1.4
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
-
key role of the enzyme in the Krebs cycle
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + phosphate + succinyl-CoA
?
show the reaction diagram
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
show the reaction diagram
ATP + 3-sulfinopropionate + CoA
ADP + phosphate + 3-sulfinopropionyl-CoA
show the reaction diagram
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
ATP + adipate + CoA
ADP + phosphate + adipyl-CoA
show the reaction diagram
-
59% activity compared to succinate
-
-
r
ATP + ATP
adenosine 5'-tetraphosphate + ADP
show the reaction diagram
-
-
-
-
ATP + butyrate + CoA
ADP + phosphate + butyryl-CoA
show the reaction diagram
-
48% activity compared to succinate
-
-
r
ATP + D-malate + CoA
ADP + phosphate + D-malyl-CoA
show the reaction diagram
ATP + glutarate + CoA
ADP + phosphate + glutaryl-CoA
show the reaction diagram
-
121% activity compared to succinate
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
show the reaction diagram
ATP + L-malate + CoA
ADP + phosphate + L-malyl-CoA
show the reaction diagram
ATP + oxalate + CoA
ADP + phosphate + oxalyl-CoA
show the reaction diagram
-
9% activity compared to succinate
-
-
r
ATP + propionate + CoA
ADP + phosphate + propionyl-CoA
show the reaction diagram
-
10% activity compared to succinate
-
-
r
ATP + succinate + CoA
?
show the reaction diagram
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
beta,gamma-Methylene adenosine triphosphate
Corresponding tetraphosphate + ?
show the reaction diagram
-
-
alpha,gamma-methylene adenosine tetraphosphate
-
GTP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
GTP + succinate + CoA
GDP + phosphate + succinyl-CoA
show the reaction diagram
UTP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
-
-
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + phosphate + succinyl-CoA
?
show the reaction diagram
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
show the reaction diagram
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
show the reaction diagram
ATP + succinate + CoA
?
show the reaction diagram
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
5,5'-dithiobis(2-nitrobenzoate)
-
-
acetate
-
-
AMP
-
-
Borohydride
inactivation, in the presence of acetyl-CoA causes near-complete loss of enzyme activity consistent with the reduction of the glutamyl-CoA thioester intermediate to 5-hydroxynorvaline, in absence of acetyl-CoA only partial inactivation, 71% activity relative to a control, occurs
Butyrate
-
-
Ca2+
-
10 mM, 75% inhibition
Co2+
-
up to 1 mM complete inhibition
CoA plus succinate
-
presence of succinate plus CoA inhibits adenosine 5'-tetraphosphate formation
-
cystine
-
-
EDTA
-
-
GSSG
-
-
Hemin
-
-
Hg2+
-
up to 1 mM complete inhibition
iodoacetamide
-
-
Iodosobenzoate
-
-
malonate
-
-
MnO4-
-
significant protection is obtained by: 1. MgATP2- and succinate, 51% 2. desulfo-CoA alone, 53% 3. MgATP2-, succinate, desulfo-CoA, 93%
NEM
-
-
Pb2+
-
up to 10 mM complete inhibibition
PCMB
-
-
Propionate
-
-
protoporphyrin IX
-
-
SDS
-
1.0 mM
Sodium arsenite
-
-
succinate
valproyl-CoA
-
45-55% inhibition at 1 mM
zinc chloride
-
-
Zn2+
-
up to 1 mM complete inhibition
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8-hydroxyquinoline
-
5 mM, enhances activity
glutathione
-
activates
NaCN
-
10 mM , enhances activity
phosphate
-
binds the porcine heart SCS alpha-subunit in a noncovalent manner and enhances its enzymatic activity. The ability of SCS alpha-subunit to retain its phosphate in SDS-PAGE is unique over the entire mitochondrial proteome. Phosphate in millimolar concentrations induces activation of SCS by more than 2fold
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5 - 2.964
3-sulfinopropionate
70
acetate
pH 8.0, 25C
0.0223
acetyl-CoA
pH 8.0, 25C
0.0077 - 0.25
ADP
0.005 - 1.6
ATP
0.0013 - 29
CoA
0.01
coenzyme A
-
-
3.588 - 4.243
D-malate
0.011 - 0.311
GTP
0.351 - 1.509
Itaconate
2.558 - 3.27
L-Malate
0.72 - 1.4
phosphate
0.141 - 14
succinate
0.0221 - 0.041
succinyl-CoA
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
3-sulfinopropionate
280
acetate
Acetobacter aceti
B3EY95
pH 8.0, 25C
75.2
acetyl-CoA
Acetobacter aceti
B3EY95
pH 8.0, 25C
22
ADP
Thermococcus kodakarensis
-
at 55C
0.57 - 2343
ATP
1.6 - 40.3
CoA
1.2 - 2.1
D-malate
0.21 - 1780
GTP
0.5 - 5.3
Itaconate
1.1 - 2.6
L-Malate
20
phosphate
Thermococcus kodakarensis
-
at 55C
0.3 - 70.9
succinate
201
succinyl-CoA
Acetobacter aceti
B3EY95
pH 8.0, 25C
additional information
additional information
Escherichia coli
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 1
3-sulfinopropionate
14.8 - 354.4
ATP
372.3 - 1100
CoA
0.3 - 0.6
D-malate
3.1 - 15.1
Itaconate
0.3 - 0.8
L-Malate
17.2 - 171.1
succinate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.053
strain 2002, reverse reaction
0.083
strain 1023, reverse reaction
0.1
Pigeon
-
-
0.114
strain 2002, forward reaction
0.17
strain 1023, forward reaction
0.18
-
cell extract
1 - 2
purified recombinant enzyme, pH 7.4, 30C, succinyl-CoA/ADP formation; purified recombinant enzyme, pH 7.4, 30C, succinyl-CoA/ADP formation
4.14
purified recombinant enzyme, pH 7.4, 30C, succinyl-CoA/ADP formation; purified recombinant enzyme, pH 7.4, 30C, succinyl-CoA/ADP formation
18.6
purified recombinant enzyme, pH 7.4, 30C, succinyl-CoA/ADP formation; purified recombinant enzyme, pH 7.4, 30C, succinyl-CoA/ADP formation
39.4
-
after 221fold purification
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
-
immobilized enzyme
7.9 - 8.3
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9.6
-
6.0: about 50% of maximal activity, 9.5: about 30% of maximal activity
7 - 9
-
about 50% of maximal activity at pH 7.0 and pH 9.0
7.1 - 9
-
pH 7.1: about 75% of maximal activity, pH 9.0: about 70% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32 - 40
-
immobilized enzyme
35
-
free enzyme
38
-
-
65
B1Y9F9 and B1Y9G0
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 60
-
about 50% of maximal activity at 15C and 60C
25 - 45
-
about 50% of maximal activity at 25C and 45C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.9
-
isoelectric focusing
8.47
-
beta-subunit, sequence calculation
8.7
subunit beta, theoretical value
9.34
-
alpha-subunit, sequence calculation
9.6
subunit alpha, theoretical value
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
low activity; muscle
Manually annotated by BRENDA team
-
two distinct ATP-specific and GTP-specific succinyl-CoA synthetases
Manually annotated by BRENDA team
-
two distinct ATP-specific and GTP-specific succinyl-CoA synthetases
Manually annotated by BRENDA team
; high level; high level
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
-
SDS-PAGE, beta subunit
35000
-
alpha-subunit, SDS-PAGE
35500
subunit alpha, theoretical value
47100
subunit beta, theoretical value
50000
-
SDS-PAGE, alpha subunit
68000
-
gel filtration
80000 - 100000
Pigeon
-
-
130000
-
gel filtration
136000
-
gel filtration
141000
-
tertameric form, sedimentation equilibrium measurement
150000
160000
170000
-
gel filtration
171000
-
gel filtration
174000
184000
-
gel filtration
330000
-
native gel electrophoresis
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
heterotetramer
-
2 * 50000 + 2 * 27000, gel filtration
tetramer
additional information
-
homology modelling using pig SCS, PDB code 2fp4, induced-fit docking calculations and molecular dynamics simulations, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by X-ray crystallography
-
detailed structural description
-
wild-type and mutant enzyme E197betaA, hanging drop vapour diffusion method
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 10
-
50C, 30 min stable
816
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
-
pH 7.5, half-life: 60 min
80
-
5 min, about 10% loss of activity
90
-
5 min, complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
25% loss of activity after 3 months at 4C, immobilized enzyme
-
ATP or phosphate protects against trypsin inactivation
-
mutant W76F and mutant W43,76,248F are more sensitive to proteolysis by clostripain than the wild type enzyme or other Trp mutant proteins. ADP and ATP both protect the enzyme against inactivation by clostripain. Mutagenic replacement of Argbeta80, but not Argbeta14, with Lys results in an enzyme that is resistant to clostripain as wild type enzyme
-
phosphorylation of 1 active site histidine residue per oligomeric enzyme molecule results in a significant change in the three-dimensional structure of the enzyme to a tighter conformation, with concomittant stability
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
stable for several months in the frozen state
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Dyematrex Blue A column chromatography and DE-52 cellulose chromatography
-
recombinant C-terminally His-tagged enzyme 1.55fold from Escherichia coli strain BL21(DE3)-pLysS by nickel affinity chromatography; recombinant C-terminally His-tagged enzyme 1.55fold from Escherichia coli strain BL21(DE3)-pLysS by nickel affinity chromatography
recombinant enzyme 1.07fold from Escherichia coli strain BL21(DE3)-pLysS by two different steps of anion exchange chromatography and affinity chromatography; recombinant enzyme 1.07fold from Escherichia coli strain BL21(DE3)-pLysS by two different steps of anion exchange chromatography and affinity chromatography
recombinant enzyme 1.47fold from Escherichia coli strain BL21(DE3)-pLysS by anion exchange and affinity chromatography; recombinant enzyme 1.47fold from Escherichia coli strain BL21(DE3)-pLysS by anion exchange and affinity chromatography
recombinant His-tagged proteins from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
recombinant His6-tagged enzyme from Escherichia coli by ammonium sulfate fractionation and metal affinity chromatography
recombinant maltose-binding protein-tagged beta-subunit of succinyl-CoA synthetase, SUCLA2, from Escherichia coli strain Top10 by amylose affinity chromatography and gel filtration
-
recombinant soluble enzyme from Escherichia coli strain BL21(DE3)/pLysS by anion exchange chromatography; recombinant soluble enzyme from Escherichia coli strain BL21(DE3)/pLysS by anion exchange chromatography
Resource Q column chromatography, Resource ISO column chromatography, and Superdex 200 HR 10/30 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha and beta subunits, expression of His-tagged proteins in Escherichia coli strain BL21(DE3), phylogenetic analysis of SCS subunits
-
beta-subunit
-
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIL cells
-
expression in Escherichia coli
expression of the maltose-binding protein-tagged beta-subunit of succinyl-CoA synthetase, SUCLA2, in Escherichia coli strain Top10
-
gene aarC, DNA and amino acid sequence determination and analysis, expression analysis, overexpression as soluble His6-tagged enzyme in Escherichia coli
gene CG11963, expression as GST-tagged enzyme in Escherichia coli strain BL21(DE3), interaction analysis of Myc-tagged CG11963 and FLAG-tagged dKCNQ using the yeast two-hybrid system
-
gene scsB, DNA and amino acid sequence determination and analysis, quantitative expression analysis in in tachyzoites and in vitro bradyzoites, overview
gene sucCD, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)/pLysS; gene sucCD, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)/pLysS
gene sucCD, expression in Escherichia coli strain BL21(DE3)-pLysS; gene sucCD, expression in Escherichia coli strain BL21(DE3)-pLysS
gene sucCD, expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)-pLysS; gene sucCD, expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)-pLysS
gene SUCLG2, DNA and amino acid sequence determination and analysis, semi quantitative RT-PCR expression analysis
-
isolation and amino terminal sequencing of 3 alpha-SCS proteins
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
approximately 10fold downregulated in presence of acetate, 4-hydroxybutyrate, succinate or pyruvate
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C123ALPHAA
-
lower catalytic efficiency compared to the wild type enzyme
C123ALPHAS
-
lower catalytic efficiency compared to the wild type enzyme
C123ALPHAT
-
lower catalytic efficiency compared to the wild type enzyme
C123ALPHAV
-
lower catalytic efficiency compared to the wild type enzyme
C325E
-
Cys325Glu mutant is 83% as active as the wild type enzyme. The mutant enzyme is refractory to chemical modification by CoA disulfide-S,S-dioxide and methyl methane thiosulfonate. It is less reactive with NEM
E197betaA
-
mutant enzyme with very low activity. The mutant protein is crystallized in the same space group as the wild-type enzyme. Crystals of the mutant enzyme grew as plates rather than as cubes which are the usual crystal habit for the wild-type enzyme
E197betaD
-
the Km-values and turnover numbers are comparable to those of the wild-type enzyme
E197betaQ
-
the KM-value for each substrate is comparable to that of the wild-type enzyme, except for GTP, whose Km-value is reduced by a factor of 20. 3000fold decrease in turnover number for reaction with ATP, 7000fold decrease in turnover-number when using GTP
E208alphaD
-
Km-values for succinate, CoA, GTP and ATP are comparable to those observed with wild-type enzyme. The turnover-numbers for ATP and GTP are comparable to the wild-type value
E208alphaQ
-
Km-values for succinate, CoA and ATP are comparable to those observed with wild-type enzyme. The KM-value for GTP is 36times lower than that of the wild-type enzyme. The turnover-numbers for ATP and GTP are reduced approximately 5000fold compared to the wild-type enzyme
E231betaA
-
activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
E231betaW
-
strong decrease in activity
E231betaW/Q247betaW/E249betaW
-
strong decrease in activity
E29betaD/E33betaA/S36betaA
-
activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact
E33betaA/S36betaA
-
activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact
E33betaA/S36betaA/K66betaA
-
activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact
E4betaK/R14betaD//R70betaG/E231betaW/Q247betaW/E24
-
strong decrease in activity
E74betaK
-
activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
H246D
-
His246alpha to Asp mutant is indistinguishable from the native enzyme with respect to its subunit assembly, but has no ability to catalyze the overall reaction. The mutant enzyme is incapable of undergoing phosphorylation and is devoid of arsenolysis activity
K66betaA
-
activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact
M156betaD/Y1258betaD/R161betaE/E162betaR
-
mutant enzyme with alphabeta-dimer subunit structure
N142N
-
mutant H142N is devoid of the ability to catalyze the overall reaction but is able to catalyze the half-reactions at significant rates. Phosphorylation by ATP and dephosphorylation by ADP of the mutant enzyme occurs at rates that are at least 10times greater than those with wild type enzyme. Dephosphorylation by succinate plus CoA, succinyl-CoA formation, proceeds with a maximal velocity of 10% that of wild type enzyme
Q247betaK
-
activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
R14betaD
-
activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
R14betaD/E231betA
-
activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
R14betaD/R70betaG/E74betaK
-
activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
R14betaD/R70betaG/E74betaK/E231betaA/Q247betaK
-
activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
R29betaA/E33betaA/S36betaA/K66betaA
-
strong decrease in activity
R29betaD
-
activity of the mutant enzyme is not significantly different from that of the wild-type enzyme, tetrameric structure remains intact
R70betaG
-
activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
R70betaG/E74betaK
-
activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
R70betaG/E74betaK/Q247betaK
-
activity of the mutant enzyme is equal to that of the wild-type enzyme, mutation fails to disrupt the tetrameric structure
W43F/W76F/W248F
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mutant W76F and mutant W43,76,248F are more sensitive to proteolysis by clostripain than the wild type enzyme or other Trp mutant proteins. Mutagenic replacement of Argbeta80, but not Argbeta14, with Lys results in an enzyme that is resistant to clostripain as wild type enzyme
W76F
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mutant W76F and mutant W43,76,248F are more sensitive to proteolysis by clostripain than the wild type enzyme or other Trp mutant proteins. Mutagenic replacement of Argbeta80, but not Argbeta14, with Lys results in an enzyme that is resistant to clostripain as wild type enzyme
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
50-60% of the activity can be recovered following renaturation. ATP is required for reconstitution
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enzyme that is completely inactivated by 0.6 M guanidine hydrochloride, but contains 90% residual native structure, can refold back to fully active enzyme. Enzyme denatured in 1.5 M and 6.0 M guanidine hydrochloride, that is catalytically inactive and devoid of a large fraction of the native enzyme structure, can also regain the native structure upon refolding, but the refolded structures are only 86% and 71% active, respectively
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purified bacterial chaperone GroEL has no effect on the folding and assembly of succinyl-CoA synthetase
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molecular biology
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the maltose-binding protein-tagged beta-subunit of succinyl-CoA synthetase, SUCLA2, bound to an amylose resin, is used as an affinity ligand to bind FPLC-purified wild-type and some mutant erythroid-specific aminolevulinic acid synthases, ALAS2
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