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1.3.5.1: succinate dehydrogenase

This is an abbreviated version!
For detailed information about succinate dehydrogenase, go to the full flat file.

Word Map on EC 1.3.5.1

Reaction

succinate
+
a quinone
=
fumarate
 +
a quinol

Synonyms

8-methylmenaquinol:fumarate reductase, AaSdhB, bacterial succinate:quinone oxidoreductase flavoprotein, complex II, Complex II homolog, complex II of the respiratory chain, complex II succinate:ubiquinone oxidoreductase, DCPIP oxidoreductase, dehydrogenase, succinate, dehydrogenase/complex II, EC 1.3.5.4, EC 1.3.99.1, Fcc3, fdrB, FL cyt, Flavocytochrome c3, FRD, FrdA, FRdABCD, FrdC, FRdCAB, FrdD, fumarate reductase, fumarate reductase complex, fumaric hydrogenase, Ifc3, Iron(III)-induced flavocytochrome C3, iron-sulfur subunit of succinate dehydrogenase, menaquinol-1 fumarate reductase, menaquinol-fumarate oxidoreductase, menaquinol:fumarate oxidoreductase, methylmenaquinol:fumarate reductase, MFR, MFR complex, MfrA, MfrB, mitochondrial complex II, mitochondrial succinate dehydrogenase, mitochondrial succinate:ubiquinone oxidoreductase, More, mQFR, MSMEG_0416, MSMEG_0417, MSMEG_0418, MSMEG_0419, MSMEG_0420, MSMEG_1669, MSMEG_1670, MSMEG_1671, MSMEG_1672, non-classical succinate:quinone reductase, QFR, quinol-fumarate reductase, quinol:fumarate reductase, SDG, SDG-1, SDG-2, SDH, SDH1, SDH2, SDH2-1, SDH2-2, SDH3, SDH4, SdhA, sdhABE, SDHB, SdhC, sdhCAB, SdhCDAB, SdhD, SDISP, SQR, succinate dehydrogenase, succinate dehydrogenase (caldariellaquinone), succinate dehydrogenase (quinone), succinate dehydrogenase B, succinate dehydrogenase complex, succinate dehydrogenase flavoprotein subunit Sdh1p, succinate dehydrogenase iron-sulfur protein, succinate dehydrogenase iron-sulphur protein, succinate dehydrogenase subunit B, succinate oxidoreductase, succinate-2,6-dichlorophenolindophenol oxidoreductase, succinate-coenzyme Q reductase, succinate-quinone oxidoreductase, succinate-quinone reductase, succinate-ubiquinone oxidoreductase, succinate:caldariellaquinone oxidoreductase, succinate:menaquinone 7-reductase, succinate:menaquinone oxidoreductase, succinate:menaquinone reductase, succinate:MK reductase, succinate:quinone oxidoreductase, succinate:quinone reductase, succinate:quinone reductases, succinate:ubiquinone oxidoreductase, succinate:ubiquinone reductase, succinic acid dehydrogenase, succinic dehydrogenase, succinodehydrogenase, succinyl dehydrogenase, Tneu_0423

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.5 With a quinone or related compound as acceptor
                1.3.5.1 succinate dehydrogenase

Engineering

Engineering on EC 1.3.5.1 - succinate dehydrogenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H277R
-
the molecular basis of boscalid-resistant phenotypes in Alternaria alternata is elucidated. Furthermore, the cross-resistance pattern between boscalid and carboxin in these isolates is investigated. The iron-sulfur subunit of SDHB is targeted for analysis. Sequence comparison of resistant isolates with those of the wild-type isolates show that a single point mutation exist in fungicide-resistant isolates. This mutation leads to a substitution of a highly conserved histidine residue, located in a region associated with the (3Fe-4S) high-potential non-heme iron sulphur-redox (S3) center to either H277Y or H277R
H277Y
-
the molecular basis of boscalid-resistant phenotypes in Alternaria alternata is elucidated. Furthermore, the cross-resistance pattern between boscalid and carboxin in these isolates is investigated. The iron-sulfur subunit of SDHB is targeted for analysis. Sequence comparison of resistant isolates with those of the wild-type isolates show that a single point mutation exist in fungicide-resistant isolates. This mutation leads to a substitution of a highly conserved histidine residue, located in a region associated with the (3Fe-4S) high-potential non-heme iron sulphur-redox (S3) center to either H277Y or H277R
G168D
-
enzyme not assembled, properties of heme bP and heme bD seem normal
H113L
-
enzyme not assembled
H113M
-
assembled enzyme, low enzyme activity, altered properties of heme bD compared to wild-type
H113Y
-
enzyme not assembled, contains heme
H13Y
-
assembles enzyme with about 50% of normal activity, alters properties of heme bP and heme bD compared to wild-type, the isolated enzyme is not stable in the presence of succinate
H155L
-
assembled enzyme, the enzyme has some activity but apparently is unstable
H155Y
-
enzyme not assembled, contains heme
H28L
-
assembles succinate dehydrogenase, active succinate dehydrogenase but inactive succinate: quinone reductase, contains heme bP but lacks low potential heme
H28Y
-
enzyme not assembled, contains heme
H47Y
-
assembles fully active enzyme
H70L
-
enzyme not assembled
H70Y
-
enzyme not assembled
H70Y/Y73S
-
assembled enzyme, enzyme activity is 30% of normal
S214C/Q215G
-
substitution in the IP subunit, mutant is enzymatically impaired and less stable than wild-type
P211F
mutant shows significant reduced SDH activity, mutant shows significant shorter life span compared to wild-type, embryogenesis is impaired in mutant (dead embryos all arrest before the four-cell stage), mutant shows an increased hypersensitivity to oxidative stress compared to wild-type, respiration rate is significantly decreased in mutant compared to wild-type, mitochondria of mutant generate significantly more superoxide compared to wild-type
P211H
mutant shows significant reduced SDH activity, mutant shows significant shorter life span compared to wild-type, embryogenesis is impaired in mutant (dead embryos all arrest before the four-cell stage), mutant shows an increased hypersensitivity to oxidative stress compared to wild-type, respiration rate is significantly decreased in mutant compared to wild-type, mitochondria of mutant generate significantly more superoxide compared to wild-type
P211L
mutant shows the weakest SDH activity, mutant shows a significant shorter life span compared to wild-type, embryogenesis is impaired in mutant (dead embryos all arrest before the four-cell stage), mutant shows an increased hypersensitivity to oxidative stress compared to wild-type, respiration rate in P211L mutant is increased compared to wild-type, mitochondria of mutant generate significantly more superoxide compared to wild-type
P211N
mutant shows significant reduced SDH activity, embryogenesis is impaired in mutant (dead embryos all arrest before the four-cell stage), mutant shows an increased hypersensitivity to oxidative stress compared to wild-type
P211Q
mutant shows significant reduced SDH activity, embryogenesis is impaired in mutant (dead embryos all arrest before the four-cell stage), mutant shows an increased hypersensitivity to oxidative stress compared to wild-type
P211R
mutant shows significant reduced SDH activity, life span of mutant is not reduced compared to wild-type, embryogenesis is impaired in mutant, in P211R mutant are twice as many dead embryos compared to wild-type (dead embryos all arrest before the four-cell stage), mutant shows an increased hypersensitivity to oxidative stress compared to wild-type, mitochondria of mutant generate significantly more superoxide compared to wild-type
C247
-
mutation in flavoprotein subunit FrdA. Increase in fumarate reduction rate, slight increase in succinate oxidation. Residue C247 of FrdA is responsible for the N-ethylmaleimide sensitivity shown by fumarate reductase but is not required for catalytic activity or the tight-binding of oxalacetate
D288N
site-directed mutagenesis, the FrdAD288N variant shows minimal residual fluorescence, suggesting covalent flavinylation is severely compromised
D95E
-
site-directed mutagenesis of subunit C, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme
D95L
-
site-directed mutagenesis of subunit C, the mutant shows a shifted pH-optimum but similar activity compared to the wild-type enzyme
E101D
-
site-directed mutagenesis of subunit C, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme
E101L
-
site-directed mutagenesis of subunit C, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme
E245Q
site-directed mutagenesis, the mutant of FrdA shows almost complete absence of covalent flavinylation. Mutant crystal structure analysis, overview
E49A
decrease in catalytic efficiency of both fumarate reduction and succinate oxidation
E49Q
decrease in catalytic efficiency of both fumarate reduction and succinate oxidation
F20L
-
growth on succinate is essentially the same as the wild-type, electron transfer activity, the apparent Km value for Q2 and the amount of azido-Q incorporated into the succinate dehydrogenase C subunit are comparable with those of the complement reductase, Phe-20 is not involved in the Q binding
G227L
-
site-directed mutagenesis of subunit B, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme
G227L/D95E
-
site-directed mutagenesis of subunits B and C, respectively, the mutant shows a shifted pH optimum compared to the wild-type enzyme and is inactive above pH 7.0
G227L/D95L
-
site-directed mutagenesis of subunits B and C, respectively, the mutant shows a shifted pH optimum compared to the wild-type enzyme and is inactive above pH 7.0
H232S
-
mutation in flavoprotein subunit FrdA. Decrease in fumarate reduction, strong decrease in succinate oxidation. Residue H232 is the general acid-base catalyst
H30A
-
growth on succinate is essentially the same as the wild-type, electron transfer activity, the apparent Km value for Q2 and the amount of azido-Q incorporated into the succinate dehydrogenase C subunit are comparable with those of the complement reductase, His-30 is not involved in the Q binding
H355S
site-directed mutagenesis, the mutant of FrdA shows almost complete absence of covalent flavinylation
H44C
-
the mutation allows cell growth in glycerol/fumarate medium at a 4fold slower rate than control cells, fumarate reductase activity: the mutant oxidizes reduced benzyl viologen with 38% of the efficiency of wild-type, succinate dehydrogenase activity: the mutant membrane complex is inactive as compared to the wild-type complex
H44R
-
the mutation does not allow cells to grow anaerobically on glycerol and fumarate, the substitution produces an inactive complex
H44S
-
the mutation allows cell growth in glycerol/fumarate medium at a 4fold slower rate than control cells, fumarate reductase activity: the mutant oxidizes reduced benzyl viologen with 32% of the efficiency of wild-type, succinate dehydrogenase activity: the mutant membrane complex is inactive as compared to the wild-type complex
H44Y
-
the mutation allows cell growth in glycerol/fumarate medium at a 7fold slower rate than control cells, fumarate reductase activity: the mutant oxidizes reduced benzyl viologen with 17% of the efficiency of wild-type, succinate dehydrogenase activity: the mutant membrane complex is inactive as compared to the wild-type complex
H71C
-
role of a Cys residue in Escherichia coli SdhD for heme b coordination is examined. H71C mutant is created to mimic the TyrCys motif found in yeast Sdh4p. Mutant H71C results in a protein that retains penta-coordinated heme b indicating that Cys is not able to provide coordination for the heme in Escherichia coli SQR even in its optimal structural position. Km (ubiquinone): 0.012 mM compared to 0.0025 mM wild-type. H71C and Y71C72 mutants show higher phenazine ethosulfate or ubiquinone reductase activities than mutant H71Y. Mutant H71C retains 43% of ubiquinone reductase activity compared to wild-type SQR, quinone reductase activity is impaired to a greater extent than its succinate-oxidase activity measured with phenazine ethosulfate
H71L
-
mutation significantly reduces the succinate-ubiquinone reductase activity of the enzyme, mutant enzyme produces more superoxide than the wild-type enzyme
H71Q
-
mutation in SdhC subunit, 82% and 69% of wild-type kcat with succinate-phenazine ethosulfate and succinate, respectively
H71Y
-
mutant lacks heme. Km (ubiquinone): 0.01 mM compared to 0.0025 mM wild-type, lower ubiquinone or phenazine ethosulfate reductase activity compared to mutant H71C or double mutant H71Y/A72C
H71Y/A72C
-
role of a Cys residue in Escherichia coli SdhD for heme b coordination is examined. H71C mutant is created to mimic the TyrCys motif found in yeast Sdh4p. Double mutant assembles within the membrane but without heme, and it retains the ability to reduce quinone. Km (ubiquinone): 0.013 mM compared to 0.0025 mM wild-type. H71C and Y71C72 mutants show higher phenazine ethosulfate or ubiquinone reductase activities than mutant H71Y. The Y71C72 double mutant shows significant improvement in its activity compared to H71Y or H71C
H82R
-
menaquinone, ubiquinone and b-type cytochrome levels are present in normal amounts, the mutation alters the electron transfer properties of the iron-sulfur and flavin redox centers of the catalytic domain, functional electron flow from 2,3-dimethyl-1,4-naphthoquinone or from the electron transport chain is impaired, the mutant can be reduced normally by single-electron donors such as benzyl viologen
H84L
-
mutation in SdhC subunit, 54% and 23% of wild-type kcat with succinate-phenazine ethosulfate and succinate, respectively
H91L
-
mutant enzyme produces more superoxide than the wild-type enzyme
I150E
-
mutation lowers the midpoint potential of the [4Fe-4S] cluster
I150H
-
mutation lowers the midpoint potential of the [4Fe-4S] cluster
I28E
-
mutation significantly reduces the succinate-ubiquinone reductase activity of the enzyme, mutant enzyme produces more superoxide than the wild-type enzyme
K228L
K228R
L220S
-
mutation does not alter the redox behavior of the [4Fe-4S] cluster but instead lowers the midpoint potential of the [3Fe-4S] cluster
Q78L
-
site-directed mutagenesis of subunit D, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme
R19A
-
growth on succinate is essentially the same as the wild-type, electron transfer activity, the apparent Km value for Q2 and the amount of azido-Q incorporated into the succinate dehydrogenase C subunit are comparable with those of the complement reductase, Arg-19 is not involved in the Q binding
R248H
-
mutation in flavoprotein subunit FrdA. Strong decrease both in fumarate reduction and in succinate oxidation
R248L
-
mutation in flavoprotein subunit FrdA. Strong decrease both in fumarate reduction and in succinate oxidation
R287K
site-directed mutagenesis, the mutant of FrdA shows almost complete absence of covalent flavinylation
R28E/E29I
mutation in subunit FrdC, retains normal level of activity
R28L
mutation in subunit FrdC, retains normal level of activity
R28L/E9L
mutation in subunit FrdC, retains normal level of activity
R28L/R81A
mutation in subunits FrdC/FrdD, loss of activtiy with ubiquinone and menaquinol
R28N
mutation in subunit FrdC, retains normal level of activity
R31A
-
the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, Arg-31 is a critical residue for succinate-Q-reductase
R31H
-
the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, the guanidino group of arginine is critical for succinate-Q reductase activity
R31K
-
the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, the guanidino group of arginine is critical for succinate-Q reductase activity, it occupies a much larger space than the primary amine of lysine, extends a longer distance, and may provide more chance for hydrogen bond formation, it may stabilize Q binding through pi-pi interactions between the guanidino group and the benzoquinone ring
R390K
site-directed mutagenesis, the mutant of FrdA shows almost complete absence of covalent flavinylation
R390Q
site-directed mutagenesis, the mutant of FrdA shows almost complete absence of covalent flavinylation
R81A
mutation in subunit FrdD, retains normal level of activity
R81E
mutation in subunit FrdD, retains normal level of activity
R81K
mutation in subunit FrdD, retains normal level of activity
S27A
-
the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, Ser-27 is a critical residue for succinate-Q-reductase, it participates in a hydrogen bond at the Q-binding site of the C subunit
S27C
-
the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, the size of the amino acid side chain at position 27 of C subunit is critical for Q binding
S27T
-
the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, the size of the amino acid side chain at position 27 of C subunit is critical for Q binding
S33A
-
the mutant has retarded aerobic growth rate in succinate/M9 medium and it has 35% of the succinate-Q-reducase activity of complement enzyme, the apparent Km value of this mutant for Q2 is about the same as wild-type, the purified mutant protein has azido-Q uptake comparable with that of complement reductase, the mutation of Ser-33 to alanine may greatly reduce enzyme turnover without affecting the affinity for Q
S33C
-
the mutant has retarded aerobic growth rate in succinate/M9 medium and it has 44% of the succinate-Q-reducase activity of complement enzyme, the apparent Km value of this mutant for Q2 is about the same as wild-type, the purified mutant protein has azido-Q uptake comparable with that of complement reductase
S33T
-
the mutant has retarded aerobic growth rate in succinate/M9 medium and it has 88% of the succinate-Q-reducase activity of complement enzyme, the apparent Km value of this mutant for Q2 is about the same as wild-type, the purified mutant protein has azido-Q uptake comparable with that of complement reductase
T17A
-
growth on succinate is essentially the same as the wild-type, electron transfer activity, the apparent Km value for Q2 and the amount of azido-Q incorporated into the succinate dehydrogenase C subunit are comparable with those of the complement reductase, Thr-17 is not involved in the Q binding
T23A
-
the mutation yields cells capable of aerobic growth on M9/succinate medium at a rate slightly slower than that of complement strain, 40% decrease in the specific activity of the mutant to catalyze electron transfer from succinate to Q, apparent Km for Q2 is the same as that of complement reductase, Thr-23 may not be involved in Q binding
A3G
-
naturally occurring germline mutation of gene SDHB, phenotype, overview
C191Y
-
a novel germline missense SDHB mutation (C191Y) in a patient affected by a glomus tumor is reported. The missense mutation hits an amino acid residue conserved from mammals to the yeast Saccharomyces cerevisiae. Histochemistry demonstrates that SDH activity is selectively absent in the patient tumor tissue
G12S
-
naturally occurring germline mutation of gene SDHD, phenotype, overview
G148D
-
naturally occuring germline mutation of the subunit D encoding gene SDHD, the mutation is involved in metastatic paragangliomas development, phenotype
H145N
-
naturally occurring germline mutation of gene SDHD, phenotype, overview
H50R
-
naturally occurring germline mutation of gene SDHD, phenotype, overview
L157X
-
the case of a novel SDHB mutation (L157X) in a Japanese patient with abdominal paraganglioma following malignant lung metastasis is reported. Novel mutation is a nonsense mutation, resulting in a truncated protein. In addition, an asymptomatic carrier of the SDHB mutation in this family is identified
L85X
-
naturally occuring germline mutation of the subunit D encoding gene SDHD, the mutation is involved in metastatic paragangliomas development, phenotype
R17X
-
naturally occuring mutation in the SDHD gene of a 29-year-old man showing metastases in both lungs and the liver, but no increased hormone production by the tumor, phenotype, overview
R46Q
-
a naturally occuring mutation in gene SDHB in a Japanese family with both abdominal and thoracic paraganglioma following metastasis
R46X
-
naturally ocurring mutations, the recurrent stop-codon mutation in succinate dehydrogenase subunit B gene might play a role in cellular pre-adaptation to hypoxia in normal peripheral blood and childhood T-cell acute leukemia, overview
S163P
-
naturally occurring germline mutation of gene SDHB, phenotype, overview
W61X
-
an unusual naturally occurring SDHC gene non-sense mutation in a case of laryngeal paraganglioma, phenotype with an additional thyroid papillary carcinoma, overview
Y114X
-
naturally occuring germline mutation of the subunit D encoding gene SDHD, the mutation is involved in metastatic paragangliomas development, phenotype
H243L
an amino-acid substitution of a highly conserved histidine residue within the third cysteine-rich cluster of SdhB replaced by a leucine residue confers carboxin resistance to the organism
B89G
-
succinate dehydrogenase D polypeptide, the mutation conferrs resistance to carboxin but not to thenoyltrifluoroacetone
C184Y
-
SDH2C184Y mutant allele equivalent to human SDHBC191Y does not restore the OXPHOS phenotype of the DELTAsdh2 null mutant. In the C184Y mutant, SDH activity is abolished along with a reduction in respiration. Sensitivity to oxidative stress is increased in the mutant, as revealed by reduced growth in the presence of menadione. The frequency of petite colony formation is increased in the C184Y mutant, indicating an increased mtDNA mutability
C630A/R638A
-
naturally occuring mutant, overexpression of Sdh5 partially does not restore growth of the double mutant
C78A/H106A
-
site-directed mutagenesis of the subunits Sdh3p and Sdh4p, leads to highly reduced to undetectable levels of heme b562 and reduced cell growth compared to the wild-type enzyme
C78H
-
mutation in Sdh4 subunit, 53% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
C85A
-
mutation in Sdh4 subunit, 94% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
D117V
-
reduced covalent FAD content
D88E
-
site-directed mutagenesis of a subunit Sdh4p residue, the mutant shows reduced activity, as well as accumulation and secretion of succinate, the mutant is sensitive to hyperoxia and paraquate and shows enhanced superoxide production in vivo and in vitro
D88K
-
site-directed mutagenesis of a subunit Sdh4p residue, the mutant shows reduced activity and FAD content
D88N
-
site-directed mutagenesis of a subunit Sdh4p residue, the mutant shows reduced activity and FAD content, as well as accumulation and secretion of succinate, the mutant is sensitive to hyperoxia and paraquate and shows enhanced superoxide production in vivo and in vitro
F103V
-
the covalent FAD level is not significantly different from the wild-type, the mutation strongly but specifically impairs quinone reductase activities but have only minor effects on enzyme assembly, Phe-103 in the Sdh3p subunit is important in the formation of a quinone-binding site in succinate dehydrogenase, the enzyme is thermolabile at temperatures above 25°C
F69V
-
mutation in anchor subunit Sdh4, 56% of wild-type kcat
G70V/R638A
-
naturally occuring Sdh1 mutant, the mutant shows slightly reduced growth without glucose
H106A
H106L/D117V
-
the covalent FAD level is reduced, indicating some impairment of enzyme assembly, quinone reductase activity is sharply reduced compared to wild-type, the enzyme is thermolabile at temperatures above 25°C
H106Y
-
the covalent FAD level is reduced, indicating some impairment of enzyme assembly, the quinone reductase activity is not greatly impaired, the enzyme is thermolabile at temperatures above 25°C
H113A
-
mutation in Sdh3 subunit, 61% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
H113Q
-
the covalent FAD level is not significantly different from the wild-type, the mutation strongly but specifically impairs quinone reductase activities but have only minor effects on enzyme assembly, His-113 in the Sdh3p subunit is important in the formation of a quinone-binding site in succinate dehydrogenase
H30A
-
mutation in Sdh3 subunit, 97% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
H37A
-
mutation in Sdh4 subunit, 100% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
H46A
-
mutation in Sdh3 subunit, 45% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
H46D
-
mutation in Sdh3 subunit, 47% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
H84A
-
mutation in Sdh3 subunit, 97% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
H99A
-
mutation in Sdh4 subunit, 75% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
K132E
-
mutation in Sdh4 subunit affects heme assembly
K132G
-
mutation in Sdh4 subunit affects heme assembly
K132Q
-
mutation in Sdh4 subunit, reduced heme content
K132V
-
mutation in Sdh4 subunit affects heme assembly
L122stop
-
the covalent FAD level is reduced, indicating some impairment of enzyme assembly, quinone reductase activity is sharply reduced compared to wild-type, the enzyme is thermolabile at temperatures above 25°C
P190Q
-
mutation in Sdh2 subunit, mutants have reduced succinate-ubiquinone oxidoreductase activity and are hypersensitive to oxygen and paraquat
R47C
-
site-directed mutagenesis of a subunit Sdh3p residue, the mutant shows reduced activity
R47E
-
site-directed mutagenesis of a subunit Sdh3p residue, the mutant shows reduced activity and FAD content
R47K
-
site-directed mutagenesis of a subunit Sdh3p residue, the mutant shows reduced activity, as well as accumulation and secretion of succinate, the mutant is sensitive to hyperoxia and paraquate and shows enhanced superoxide production in vivo and in vitro
R582A
-
site-directed mutagenesis, inactive mutant, no growth without glucose
R582A/M599R
-
the mutant shows slightly reduced growth without glucose
R582C
-
site-directed mutagenesis, the mutant shows slightly reduced growth without glucose
R582W
R638A
-
naturally occuring mutant, the mutant shows highly reduced growth without glucose, overexpression of Sdh5 partially restores growth of the single R638A mutant
S71A
-
mutation in anchor subunit Sdh4, 43% of wild-type kcat
S94E
-
mutation in Sdh4 subunit, mutants have reduced succinate-ubiquinone oxidoreductase activity and are hypersensitive to oxygen and paraquat
W116R
-
the covalent FAD level is not significantly different from the wild-type, the mutation strongly but specifically impairs quinone reductase activities but have only minor effects on enzyme assembly, Trp-116 in the Sdh3p subunit is important in the formation of a quinone-binding site in succinate dehydrogenase
Y89OCH
-
substitution with stop codon truncates Sdh4 by removing the third predicted transmembrane segment, 22% of wild-type activity
E180Q
-
site-diirected mutagenesis, the mutant catalyzes the electron transfer from succinate to methylene blue, but not from 2,3-dimethyl-1,4-naphthoquinol to fumarate
E66Q
-
site-diirected mutagenesis, the mutant catalyzes the electron transfer from succinate to methylene blue, but not from 2,3-dimethyl-1,4-naphthoquinol to fumarate
H44E
-
site-diirected mutagenesis, although the H44E variant enzyme retains both heme groups, it is unable to catalyze quinol oxidation, the mutant catalyzes the electron transfer from succinate to methylene blue, with reduced activity compared to the wild-type enzyme but not from 2,3-dimethyl-1,4-naphthoquinol to fumarate
H229Y
additional information