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

1.3.5.1

paragangliomas

fiber

malate

atpase

citrate

light-harvesting

tricarboxylic

pheochromocytoma

germline

histocompatibility

isocitrate

glycogen

3-nitropropionic

photosystems

wistar

lhcii

fungicide

chlorophyl

tca

triphosphatase

krebs

flavoproteins

histochemistry

soleus

bioenergetics

thylakoids

huntington

striatal

gastrocnemius

cytochemical

mtdna

aconitase

glucose-6-phosphatase

antenna

rotenone

gist

antimycin

oxphos

lateralis

vastus

myofibrillar

supercomplexes

submitochondrial

hippel-lindau

fast-twitch

pdgfra

subsarcolemmal

plantaris

non-photochemical

excitonic

biotechnology

medicine

diagnostics

molecular biology

Reaction

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

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Results	in table
46	Activating Compound
53874	AA Sequence
21	Application
3	CAS Registry Number
60	Cloned(Commentary)
221	Cofactor
29	Crystallization (Commentary)
6447	Disease/ Diagnostics
17	Expression
106	General Information
5	General Stability
80	IC50 Value
267	Inhibitors
5	kcat/KM [mM/s]
78	Ki Value [mM]
149	KM Value [mM]
186	Localization
105	Metals/Ions
147	Molecular Weight [Da]
127	Natural Substrates/ Products (Substrates)
821	Organism
2	Oxidation Stability
42	Pathway
234	PDB ID
49	pH Optimum
5	pH Range
5	pH Stability
8	pI Value
24	Posttranslational Modification
188	Protein Variants
58	Purification (Commentary)
3	Reaction
3	Reaction Type
359	Reference
5	Renatured (Commentary)
132	Source Tissue
52	Specific Activity [micromol/min/mg]
15	Storage Stability
394	Substrates and Products (Substrate)
141	Subunits
455	Synonyms
1	Systematic Name
45	Temperature Optimum [°C]
2	Temperature Range [°C]
11	Temperature Stability [°C]
117	Turnover Number [1/s]

Posttranslational Modification

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Posttranslational Modification on EC 1.3.5.1 - succinate dehydrogenase

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acetylation

3 entries

acylation

Thermus thermophilus

the posttranslational modification is reported to occur in SDHA subunit of Thermus thermophilus. The minor overlap observed between lysine propionylation and acetylation sites in 67 proteins that are both acetylated and propionylated suggests that the two acylation reactions are most likely regulated independently by distinct enzymes and are possibly involved in different functions

flavoprotein

lipoprotein

phosphoprotein

side-chain modification

2 entries

succinylation

Homo sapiens

P31040; P21912; Q99643; O14521

the posttranslational modification converts the cationic lysine side chain to an anion with diverse implications for protein structure and function. Systematic profiling of the mammalian succinylome, identifies SDHA and SDHB as two succinylated proteins. Most of the succinylation sites identified across the succinylome have no overlap with acetylation sites, suggesting differential regulation of succinylation and acetylation

762781

additional information

11 entries

FGR tyrosine kinase is one of the kinases that target SDHA at positions Y535 and Y596 (of rat sequence). ROS mediates the activation of FGR tyrosine kinase which phosphorylates SDHA at Y604 and that this function of FGR is required for the adjustment of metabolism under various conditions such as nutrient restriction, hypoxia/reoxygenation, and T-cell activation. This regulation together with the function of phagosomal NADPH oxidase (a source of ROS generation) seems to be essential for the activation of anti-bacterial response in macrophages through committing complex I and II (SDH) to respiration rather than their assembly. Additional to FGR, c-Src is another mitochondrial tyrosine kinase which targets both NDUFV2 (NADH dehydrogenase [ubiquinone] flavoprotein 2) at Tyr193 of respiratory complex I and SDHA at Tyr215 of complex II. NDUFV2 phosphorylation is required for NADH dehydrogenase activity, which affects both respiration and cellular ATP content. SDHA phosphorylation, on the other hand, does not alter the enzyme activity but disconcerts electron transfer resulting in the generation of reactive oxygen species. The T98G cell line and the primary neurons expressing the mutants at the corresponding Tyr residues loose viability. These observations thus propound that the mitochondrial c-Src modulates oxidative phosphorylation by phosphorylating two respiratory components and that c-Src activity is essential for cell viability. Dephosphorylation of SDHA is exemplified by PTEN-like mitochondrial phosphatase-1 (PTPMT1), an enzyme which dephosphorylates phosphatidylglycerol phosphate (in cardiolipin biogenesis pathway) and SDHA. Inhibition of PTPMT1 leads to enhanced phosphorylation and activation of SDH and consequently lower glucose concentration. Increased SDH activity lowers glucose levels by at least two mechanisms, by inducing glucose uptake and by boosting the rate of glucose utilization. Collectively these results suggest that PTPMT1 is a major coordinator of glucose utilization by mitochondria

762781