Information on EC 1.3.99.1 - succinate dehydrogenase

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

EC NUMBER
COMMENTARY hide
1.3.99.1
deleted, the activty is included in EC 1.3.5.1, succinate dehydrogenase (quinone)
RECOMMENDED NAME
GeneOntology No.
succinate dehydrogenase
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
single copy sdhB gene, encoding the iron-sulfur protein (Ip) subunit of succinate dehydrogenase, Sdh
UniProt
Manually annotated by BRENDA team
single copy sdhB gene, encoding the iron-sulfur protein (Ip) subunit of succinate dehydrogenase, Sdh
UniProt
Manually annotated by BRENDA team
gene sdh2s
-
-
Manually annotated by BRENDA team
gene SDH2-2, encoding the iron sulfur subunit of the succinate dehydrogenase protein complex
UniProt
Manually annotated by BRENDA team
two SDG isoforms with different electrophoretic mobility
-
-
Manually annotated by BRENDA team
two SDG isoforms with different electrophoretic mobility
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
gene sdh1-2
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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
fumarate + reduced acceptor
succinate + acceptor
show the reaction diagram
-
the obligate autotroph requires fumarate reductase activity if it performs CO2 fixation via a reductive citric acid cycle
-
-
r
fumarate + reduced benzyl viologen
succinate + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
r
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
r
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
fumarate + reduced acceptor
succinate + acceptor
show the reaction diagram
-
the obligate autotroph requires fumarate reductase activity if it performs CO2 fixation via a reductive citric acid cycle
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Br-
-
activates
Cl-
-
activates
Iron-sulfur cluster
K+
-
activates
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
-
-
oxaloacetic acid
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-oxobutyrate
-
-
alpha-glycerophosphate
-
-
isocitrate
-
-
protein SDHA F2
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the factor is needed for assembly and activity of SDH and also for normal root elongation, sequence diversity and conservation of SDHA F2 across kingdoms, phylogenetic analysis, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06 - 0.08
fumarate
0.3 - 0.5
succinate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
Shewanella frigidimarina (strain NCIMB 400)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 63000, SDS-PAGE
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
flavoprotein
covalent flavinylation of succinate dehydrogenase subunit A requires heat and dicarboxylic acids
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme by ammonium sulfate fractionation and gel filtration followed by anion exchange chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene sdh2, disruption of the SDH2 gene and transformation into the sdh1 mutant strain, resulting in SDH-negative strain B2S
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gene SDH2-2, expression analysis, antisense expressionin transgenic Solanum lycopersicumplants by Agrobacterium tumefaciens-mediated transformation
gene sdhB, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Hfq protein binds NrrF (a Fur-regulated sRNA) and mediates Fur-dependent NrrF regulation of succinate dehydrogenase. NrrF forms a duplex with a region of complementarity within the sdhDA region of the succinate dehydrogenase transcript, and Hfq enhances the binding of this sRNA to the identified target in the sdhCDAB mRNA. This is likely to result in rapid turnover of the transcript in vivo
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higher content of calcium cations in the nucleus correlates with the lower level of the sdh1-2 gene transcription, regulation, overview
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transcriptional regulation: the cAMP-dependent regulator GlxR functions as a repressor sdhCAB operon expression
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transcriptional regulation: the regulator of acetate metabolism RamAas functions an activator of sdhCAB operon expression, whereas RamB has no obvious influence
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treatment of K-562 cell lines with nicotinamide and kaempferol to inhibit deacetylase activity of SIRT3 and stimulate SIRT3 expression, overview
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white or red light are down-regulating factors for the mRNA content of the sdh1-2 and sdh2-3 genes and SDH catalytic activity both in wild-type plants and in the mutant deficient in the phytochrome B gene, but not in the mutant deficient in the phytochrome A gene, while the far red light of 730 nm reverses the red light effect
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C630A/R638A
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naturally occuring mutant, overexpression of Sdh5 partially does not restore growth of the double mutant
G70V/R638A
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naturally occuring Sdh1 mutant, the mutant shows slightly reduced growth without glucose
R582A
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site-directed mutagenesis, inactive mutant, no growth without glucose
R582A/M599R
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the mutant shows slightly reduced growth without glucose
R582C
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site-directed mutagenesis, the mutant shows slightly reduced growth without glucose
R582W
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naturally occuring mutant, inactive Sdh1 mutant; site-directed mutagenesis, inactive mutant, no growth without glucose
R638A
-
naturally occuring mutant, the mutant shows highly reduced growth without glucose, overexpression of Sdh5 partially restores growth of the single R638A mutant
additional information
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