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Synonyms
sucla2, succd, a-scs, cg11963, scact, adp-forming succinyl-coa synthetase, scs-betaa, a-stk, succinyl-coa synthetase (adp-forming), succinyl-coa ligase (atp-forming),
more
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ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
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r
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
additional information
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ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
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ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
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ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
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ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
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ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
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ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
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r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
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r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
the enzyme is part of the Krebs cycle
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additional information
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succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. GTP-specific succinate:CoA ligase, EC 6.2.1.4
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additional information
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succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. GTP-specific succinate:CoA ligase, EC 6.2.1.4
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additional information
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succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. GTP-specific succinate:CoA ligase, EC 6.2.1.4
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additional information
?
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deficiency of the ADP-forming succinyl-CoA synthase activity is associated with encephalomyopathy and mitochondrial DNA depletion
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?
additional information
?
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succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. GTP-specific succinate:CoA ligase, EC 6.2.1.4
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?
additional information
?
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succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. GTP-specific succinate:CoA ligase, EC 6.2.1.4
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?
additional information
?
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succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. GTP-specific succinate:CoA ligase, EC 6.2.1.4
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additional information
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the enzyme beta-subunit binds strongly to wild-type erythroid-specific aminolevulinic acid synthase, but not to the mutants M567V and S568G, aminolevulinic acid synthase mutant R452C shows binding to the succinyl-CoA synthetase, but with reduced affinity and positive cooperativity for succinyl-CoA
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ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
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-
-
r
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
additional information
?
-
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
-
-
-
-
r
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
the enzyme is part of the Krebs cycle
-
-
?
additional information
?
-
-
succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. GTP-specific succinate:CoA ligase, EC 6.2.1.4
-
-
?
additional information
?
-
succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. GTP-specific succinate:CoA ligase, EC 6.2.1.4
-
-
?
additional information
?
-
succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. GTP-specific succinate:CoA ligase, EC 6.2.1.4
-
-
?
additional information
?
-
-
deficiency of the ADP-forming succinyl-CoA synthase activity is associated with encephalomyopathy and mitochondrial DNA depletion
-
-
?
additional information
?
-
-
succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. GTP-specific succinate:CoA ligase, EC 6.2.1.4
-
-
?
additional information
?
-
succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. GTP-specific succinate:CoA ligase, EC 6.2.1.4
-
-
?
additional information
?
-
succinate-CoA ligase catalyses the reversible conversion of succinyl-CoA and ADP or GDP to succinate and ATP or GTP, cf. GTP-specific succinate:CoA ligase, EC 6.2.1.4
-
-
?
additional information
?
-
the enzyme beta-subunit binds strongly to wild-type erythroid-specific aminolevulinic acid synthase, but not to the mutants M567V and S568G, aminolevulinic acid synthase mutant R452C shows binding to the succinyl-CoA synthetase, but with reduced affinity and positive cooperativity for succinyl-CoA
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-
?
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Acidosis, Lactic
Neonatal lactic acidosis with methylmalonic aciduria by novel mutations in the SUCLG1 gene.
Acidosis, Lactic
Succinyl-CoA synthetase (SUCLA2) deficiency in two siblings with impaired activity of other mitochondrial oxidative enzymes in skeletal muscle without mitochondrial DNA depletion.
Acidosis, Lactic
SUCLA2 mutations are associated with mild methylmalonic aciduria, Leigh-like encephalomyopathy, dystonia and deafness.
Anemia, Sideroblastic
Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is disrupted in sideroblastic anemia.
Cardiomyopathy, Hypertrophic
Succinate-CoA ligase deficiency due to mutations in SUCLA2 and SUCLG1: phenotype and genotype correlations in 71 patients.
Crohn Disease
Influences of XDH genotype by gene-gene interactions with SUCLA2 for thiopurine-induced leukopenia in Korean patients with Crohn's disease.
Deafness
A Novel SUCLA2 Mutation Presenting as a Complex Childhood Movement Disorder.
Deafness
Biochemical and genetic analysis of 3-methylglutaconic aciduria type IV: a diagnostic strategy.
Deafness
Disorders caused by deficiency of succinate-CoA ligase.
Deafness
Dystonia and deafness due to SUCLA2 defect; Clinical course and biochemical markers in 16 children.
Deafness
Exclusive neuronal expression of SUCLA2 in the human brain.
Deafness
Novel mutation in SUCLA2 identified on sequencing analysis.
Deafness
SUCLA2 Arg407Trp mutation can cause a nonprogressive movement disorder - deafness syndrome.
Deafness
SUCLA2 mutations are associated with mild methylmalonic aciduria, Leigh-like encephalomyopathy, dystonia and deafness.
Down Syndrome
Co-occurring Down syndrome and SUCLA2-related mitochondrial depletion syndrome.
Dystonia
Biochemical and genetic analysis of 3-methylglutaconic aciduria type IV: a diagnostic strategy.
Dystonia
Dystonia and deafness due to SUCLA2 defect; Clinical course and biochemical markers in 16 children.
Dystonia
Exclusive neuronal expression of SUCLA2 in the human brain.
Dystonia
Novel mutation in SUCLA2 identified on sequencing analysis.
Dystonia
SUCLA2 mutations are associated with mild methylmalonic aciduria, Leigh-like encephalomyopathy, dystonia and deafness.
Epilepsy
Succinate-CoA ligase deficiency due to mutations in SUCLA2 and SUCLG1: phenotype and genotype correlations in 71 patients.
Leukopenia
Influences of XDH genotype by gene-gene interactions with SUCLA2 for thiopurine-induced leukopenia in Korean patients with Crohn's disease.
Mitochondrial Diseases
Exclusive neuronal expression of SUCLA2 in the human brain.
Mitochondrial Diseases
Mitochondrial encephalomyopathy and retinoblastoma explained by compound heterozygosity of SUCLA2 point mutation and 13q14 deletion.
Mitochondrial Diseases
Novel mutation in SUCLA2 identified on sequencing analysis.
Mitochondrial Diseases
SUCLA2 mutations cause global protein succinylation contributing to the pathomechanism of a hereditary mitochondrial disease.
Mitochondrial Diseases
[Diagnosis of mitochondrial disorders in children with next generation sequencing].
Mitochondrial Encephalomyopathies
Expanding the phenotypic spectrum of Succinyl-CoA ligase deficiency through functional validation of a new SUCLG1 variant.
Mitochondrial Encephalomyopathies
Mitochondrial encephalomyopathy and retinoblastoma explained by compound heterozygosity of SUCLA2 point mutation and 13q14 deletion.
Mitochondrial Encephalomyopathies
Mitochondrial encephalomyopathy with elevated methylmalonic acid is caused by SUCLA2 mutations.
Movement Disorders
A Novel SUCLA2 Mutation Presenting as a Complex Childhood Movement Disorder.
Movement Disorders
SUCLA2 Arg407Trp mutation can cause a nonprogressive movement disorder - deafness syndrome.
Muscle Hypotonia
A Novel SUCLA2 Mutation Presenting as a Complex Childhood Movement Disorder.
Muscle Hypotonia
Disorders caused by deficiency of succinate-CoA ligase.
Muscle Hypotonia
Dystonia and deafness due to SUCLA2 defect; Clinical course and biochemical markers in 16 children.
Muscle Hypotonia
Mitochondrial DNA Depletion Syndromes: Review and Updates of Genetic Basis, Manifestations, and Therapeutic Options.
nadh:ubiquinone reductase (h+-translocating) deficiency
Biochemical and genetic analysis of 3-methylglutaconic aciduria type IV: a diagnostic strategy.
Porphyrias, Hepatic
Physiological roles of animal succinate thiokinases. Specific association of the guanine nucleotide-linked enzyme with haem biosynthesis.
Prostatic Neoplasms
Pharmacologically targetable vulnerability in prostate cancer carrying RB1-SUCLA2 deletion.
Retinoblastoma
Mitochondrial encephalomyopathy and retinoblastoma explained by compound heterozygosity of SUCLA2 point mutation and 13q14 deletion.
succinate-coa ligase (adp-forming) deficiency
SUCLA2 Deficiency: A Deafness-Dystonia Syndrome with Distinctive Metabolic Findings (Report of a New Patient and Review of the Literature).
succinate-coa ligase (gdp-forming) deficiency
Novel mutation in SUCLA2 identified on sequencing analysis.
succinate-coa ligase (gdp-forming) deficiency
Succinate-CoA ligase deficiency due to mutations in SUCLA2 and SUCLG1: phenotype and genotype correlations in 71 patients.
succinate-coa ligase (gdp-forming) deficiency
SUCLA2 mutations are associated with mild methylmalonic aciduria, Leigh-like encephalomyopathy, dystonia and deafness.
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malfunction
in patients with enzyme mutations, muscle histology shows severe lipid accumulation, and a marked type I fibre predominance is found, with an increased variability in fibre diameter. mtDNA depletion in succinate-CoA ligase deficiency
metabolism
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key role of the enzyme in the Krebs cycle
malfunction
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knockdown of SUCLG2 by shRNA in both SUCLA2-related mitochondrial DNA depletion syndrome patient and control fibroblasts results in a significant decrease in mtDNA amount, decreased NDPK and cytochrome c oxidase activities, and a marked growth impairment, phenotype, overview
malfunction
in patients with enzyme mutations, muscle histology shows severe lipid accumulation, and a marked type I fibre predominance is found, with an increased variability in fibre diameter. mtDNA depletion in succinate-CoA ligase deficiency
malfunction
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inhibition of the enzyme might influence the activity of nucleoside diphosphate kinase inducing an imbalance of nucleotides in the mitochondria and eventually mitochondrial DNA depletion. This may account for the potential liver failure associated with valproate therapy, reported in patients with deficiencies within the mitochondrial DNA replicase system such as polymerase gamma 1
malfunction
enzyme mutations cause the encephalomyopathic mitochondrial DNA depletion syndrome with methylmalonic aciduria
malfunction
enzyme mutations result in succinyl-CoA ligase (ATP-forming) or succinyl-CoA synthetase (ADP-forming) deficiency, a mitochondrial tricarboxylic acid cycle disorder
physiological function
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SUCLG2, to a higher degree than SUCLA2, EC 6.2.1.4, is crucial for mtDNA maintenance involving mitochondrial NDPK
physiological function
probable role of an aminolevulinic acid synthase ALAS2-succinyl-CoA synthetase complex in the regulation of erythroid heme biosynthesis
physiological function
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the enzme is bound to the nucleoside diphosphate kinase, which is responsible for the mitochondrial (deoxy)nucleotide synthesis
additional information
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the GDP-dependent isozyme SUCLG2 can complement the SUCLA2-related mitochondrial DNA depletion syndrome, a result of mutations in the beta subunit of the ADP-dependent isoform SUCLA2, EC 6.2.1.4
additional information
C-terminal mutations in the erythroid-specific aminolevulinic acid synthase gene ALAS2 cause loss of binding to the beta-subunit of succinyl-CoA synthetase, SUCLA2, resulting in reduced mitochondrial enzymatic activity and X-linked sideroblastic anemia
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heterodimer
the enzyme is composed of an alpha subunit, encoded by SUCLG1, and a beta subunit, encoded by either SUCLA2 or SUCLG2. The alpha-subunit forms a heterodimer with either of its beta-subunits, resulting in an ADP-forming succinate-CoA ligase, EC 6.2.1.5, and a GDP-forming succinate-CoA ligase, EC 6.2.1.4, respectively
heterodimer
the enzyme is composed of an alpha subunit, encoded by SUCLG1, and a beta subunit, encoded by either SUCLA2 or SUCLG2. The alpha-subunit forms a heterodimer with either of its beta-subunits, resulting in an ADP-forming succinate-CoA ligase, EC 6.2.1.5, and a GDP-forming succinate-CoA ligase, EC 6.2.1.4, respectively
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A103D
the mutation is associated with encephalomyopathic mitochondrial DNA depletion syndrome
A307V
the mutation is associated with succinyl-CoA ligase (ATP-forming) or succinyl-CoA synthetase (ADP-forming) deficiency
G424D
the mutation is associated with encephalomyopathic mitochondrial DNA depletion syndrome
I402Y
the mutation is associated with encephalomyopathic mitochondrial DNA depletion syndrome
M329V
the mutation is associated with succinyl-CoA ligase (ATP-forming) or succinyl-CoA synthetase (ADP-forming) deficiency
R284C
the mutation is associated with encephalomyopathic mitochondrial DNA depletion syndrome
R40T
the mutation is associated with encephalomyopathic mitochondrial DNA depletion syndrome
V370E
the mutation is associated with encephalomyopathic mitochondrial DNA depletion syndrome
additional information
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naturally occuring mutations g.32720del43ins5 and IVS4+1G>A cause succinate-CoA ligase deficiency
additional information
naturally occuring mutations g.32720del43ins5 and IVS4+1G>A cause succinate-CoA ligase deficiency
additional information
naturally occuring mutations g.32720del43ins5 and IVS4+1G>A cause succinate-CoA ligase deficiency
additional information
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patients with SUCLA2 mutations are expected to retain the activity of G-SUCL, and only the ATP production is expected to be compromised. In addition, in patients with SUCLA2 mutations, no liver symptoms are reported. The lactate level in patients with SUCLA2 mutations is normal or moderately elevated, phenotype, overview
additional information
patients with SUCLA2 mutations are expected to retain the activity of G-SUCL, and only the ATP production is expected to be compromised. In addition, in patients with SUCLA2 mutations, no liver symptoms are reported. The lactate level in patients with SUCLA2 mutations is normal or moderately elevated, phenotype, overview
additional information
patients with SUCLA2 mutations are expected to retain the activity of G-SUCL, and only the ATP production is expected to be compromised. In addition, in patients with SUCLA2 mutations, no liver symptoms are reported. The lactate level in patients with SUCLA2 mutations is normal or moderately elevated, phenotype, overview
additional information
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the GDP-dependent isozyme SUCLG2 can complement the SUCLA2-related mitochondrial DNA depletion syndrome, a result of mutations in the beta subunit of the ADP-dependent isoform SUCLA2, EC 6.2.1.4
additional information
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naturally occuring mutations g.32720del43ins5 and IVS4+1G>A cause succinate-CoA ligase deficiency
additional information
naturally occuring mutations g.32720del43ins5 and IVS4+1G>A cause succinate-CoA ligase deficiency
additional information
naturally occuring mutations g.32720del43ins5 and IVS4+1G>A cause succinate-CoA ligase deficiency
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Elpeleg, O.; Miller, C.; Hershkovitz, E.; Bitner-Glindzicz, M.; Bondi-Rubinstein, G.; Rahman, S.; Pagnamenta, A.; Eshhar, S.; Saada, A.
Deficiency of the ADP-forming succinyl-CoA synthase activity is associated with encephalomyopathy and mitochondrial DNA depletion
Am. J. Hum. Genet.
76
1081-1086
2005
Homo sapiens
brenda
Ostergaard, E.
Disorders caused by deficiency of succinate-CoA ligase
J. Inherit. Metab. Dis.
31
226-229
2008
Homo sapiens, Homo sapiens (P53597), Homo sapiens (Q9P2R7)
brenda
Miller, C.; Wang, L.; Ostergaard, E.; Dan, P.; Saada, A.
The interplay between SUCLA2, SUCLG2, and mitochondrial DNA depletion
Biochim. Biophys. Acta
1812
625-629
2011
Homo sapiens
brenda
Bishop, D.F.; Tchaikovskii, V.; Hoffbrand, A.V.; Fraser, M.E.; Margolis, S.
X-linked sideroblastic anemia due to carboxyl-terminal ALAS2 mutations that cause loss of binding to the beta-subunit of succinyl-CoA synthetase (SUCLA2)
J. Biol. Chem.
287
28943-28955
2012
Homo sapiens (Q9P2R7)
brenda
Luis, P.B.; Ruiter, J.; Ijlst, L.; de Almeida, I.T.; Duran, M.; Wanders, R.J.; Silva, M.F.
Valproyl-CoA inhibits the activity of ATP- and GTP-dependent succinate:CoA ligases
J. Inherit. Metab. Dis.
37
353-357
2013
Homo sapiens
brenda
Luis, P.; Ruiter, J.; IJlst, L.; De Almeida, I.; Duran, M.; Wanders, R.; Silva, M.
Valproyl-CoA inhibits the activity of ATP- and GTP-dependent succinate CoA ligases
J. Inherit. Metab. Dis.
37
353-357
2014
Homo sapiens
brenda
Carrozzo, R.; Verrigni, D.; Rasmussen, M.; de Coo, R.; Amartino, H.; Bianchi, M.; Buhas, D.; Mesli, S.; Naess, K.; Born, A.P.; Woldseth, B.; Prontera, P.; Batbayli, M.; Ravn, K.; Joensen, F.; Cordelli, D.M.; Santorelli, F.M.; Tulinius, M.; Darin, N.; Duno, M.; Jouvencel, P.; Burlina, A.; Stangoni, G.; , B.
Succinate-CoA ligase deficiency due to mutations in SUCLA2 and SUCLG1 phenotype and genotype correlations in 71 patients
J. Inherit. Metab. Dis.
39
243-252
2016
Homo sapiens (Q9P2R7), Homo sapiens
brenda
Huang, X.; Bedoyan, J.K.; Demirbas, D.; Harris, D.J.; Miron, A.; Edelheit, S.; Grahame, G.; DeBrosse, S.D.; Wong, L.J.; Hoppel, C.L.; Kerr, D.S.; Anselm, I.; Berry, G.T.
Succinyl-CoA synthetase (SUCLA2) deficiency in two siblings with impaired activity of other mitochondrial oxidative enzymes in skeletal muscle without mitochondrial DNA depletion
Mol. Genet. Metab.
120
213-222
2017
Homo sapiens (Q9P2R7)
brenda