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Escherichia coli K-12 substr. MG1655 Polypeptide: succinyl-CoA synthetase, β subunit



Gene: sucC Accession Numbers: EG10981 (EcoCyc), b0728, ECK0716

Synonyms: β subunit

Regulation Summary Diagram: ?

Component of: succinyl-CoA synthetase (extended summary available)

Summary:
SucC is the β subunit of succinyl-CoA synthetase.

Trp45 and His50 are required for activity [Buck89], while Cys47 [Buck89] and Cys325 [Mann89] are not essential. Single mutations of tryptophan residues W43, W76 and W248 have little effect on enzyme activity. W76 and W248 may be part of the CoA binding site [Nishimura90]. Glu197 is essential for phosphorylation and dephosphorylation of the active site His246 in the α subunit [Fraser02].

Based on photolabeling, site-directed mutagenesis, and crystal structures, the nucleotide binding site resides in the N-terminal ATP-grasp fold of the β subunit [Joyce99, Joyce00].

SucC levels are elevated at low pH [Stancik02].

Citations: [Nishimura93]

Gene Citations: [Wood84, Magnusson86, Cunningham98a]

Locations: cytosol

Map Position: [762,237 -> 763,403] (16.43 centisomes)
Length: 1167 bp / 388 aa

Molecular Weight of Polypeptide: 41.393 kD (from nucleotide sequence), 41.0 kD (experimental) [Buck86 ]

pI: 5.59

Unification Links: ASAP:ABE-0002483 , CGSC:17845 , DIP:DIP-31852N , EchoBASE:EB0974 , EcoGene:EG10981 , EcoliWiki:b0728 , ModBase:P0A836 , OU-Microarray:b0728 , PortEco:sucC , PR:PRO_000024004 , Pride:P0A836 , Protein Model Portal:P0A836 , RefSeq:NP_415256 , RegulonDB:EG10981 , SMR:P0A836 , String:511145.b0728 , UniProt:P0A836

Relationship Links: InterPro:IN-FAMILY:IPR005809 , InterPro:IN-FAMILY:IPR005811 , InterPro:IN-FAMILY:IPR011761 , InterPro:IN-FAMILY:IPR013650 , InterPro:IN-FAMILY:IPR013815 , InterPro:IN-FAMILY:IPR013816 , InterPro:IN-FAMILY:IPR016102 , InterPro:IN-FAMILY:IPR017866 , Panther:IN-FAMILY:PTHR11815 , PDB:Structure:1CQI , PDB:Structure:1CQJ , PDB:Structure:1JKJ , PDB:Structure:1JLL , PDB:Structure:1SCU , PDB:Structure:2NU6 , PDB:Structure:2NU7 , PDB:Structure:2NU8 , PDB:Structure:2NU9 , PDB:Structure:2NUA , PDB:Structure:2SCU , Pfam:IN-FAMILY:PF00549 , Pfam:IN-FAMILY:PF08442 , Prosite:IN-FAMILY:PS01217 , Prosite:IN-FAMILY:PS50975

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006099 - tricarboxylic acid cycle Inferred from experiment Inferred by computational analysis [UniProtGOA12, UniProtGOA11a, GOA06, Buck86]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
Molecular Function: GO:0004775 - succinate-CoA ligase (ADP-forming) activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, Buck86]
GO:0005515 - protein binding Inferred from experiment [Lasserre06, Arifuzzaman06]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0000287 - magnesium ion binding Inferred by computational analysis [GOA06]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
GO:0016874 - ligase activity Inferred by computational analysis [UniProtGOA11a]
GO:0030145 - manganese ion binding Inferred by computational analysis [GOA06]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a, GOA01a]
Cellular Component: GO:0005737 - cytoplasm Inferred from experiment [Lasserre06]
GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]
GO:0009361 - succinate-CoA ligase complex (ADP-forming) Inferred from experiment [Wolodko94]

MultiFun Terms: metabolism energy metabolism, carbon TCA cycle

Essentiality data for sucC knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Subunit of: succinyl-CoA synthetase

Subunit composition of succinyl-CoA synthetase = [SucD]2[SucC]2
         succinyl-CoA synthetase, α subunit = SucD (summary available)
         succinyl-CoA synthetase, β subunit = SucC (summary available)

Summary:
Succinyl-CoA synthetase catalyzes the only reaction of the TCA cycle that employs substrate-level phosphorylation. The reaction is reversible and is thought to proceed in three partial reactions via enzyme-bound succinyl-phosphate and a phosphorylated enzyme intermediate, where a histidine residue of the α subunit is transiently phosphorylated. Many biochemical studies were done with the enzyme purified from E. coli Crooks strain (see citations in the Enzymatic Reaction summary), while mutant enzymes were obtained from the genes of a K-12-derived strain.

A hybrid enzyme containing one wild-type and one catalytically inactive α subunit retains significant enzymatic activity, arguing for the presence of two independently active heterodimers [Mann91]. Crystal structures of the enzyme from various E. coli sources have been solved [Wolodko84, Wolodko94, Fraser99b, Joyce00, Fraser02, Hidber07]. The α2β2 heterotetramer is composed of two αβ heterodimers [Wolodko94]. Two possible alternative interpretations of the dimer-dimer interface were resolved by generating site-directed mutants that exist and are catalytically active as αβ heterodimers [Bailey99].

Overlap of the sucC and sucD open reading frames suggests translational coupling [Buck85].

A sucCD insertion mutant does not grow aearobically on acetate or α-ketoglutarate or anaerobically on glucose or succinate as carbon sources. Expression of sucCD is higher under aerobic than anaerobic conditions and is induced by growth on acetate [MatJan89a]. A sucCD deletion mutant shows higher acetate accumulation and lower biomass formation than wild type on glucose minimal medium and can not re-utilize acetate that is secreted during growth on glucose [Veit07]. sucCD and sucAB are mutually essential. Both sets of genes encode an enzyme that can produce succinyl-CoA, an essential precursor for peptidoglycan biosynthesis; deletion of either set alone results in a longer lag phase, while cells where both sets are deleted are not viable [Yu06].

Reviews: [Nishimura86, Bridger87, Miles87b]

Citations: [Grinnell69a, Grinnell70, Thomas74, Pearson75a, Krebs74, Leitzmann70, Bridger71, Bridger68, OConnorMcCourt85, Buck86, Wolodko86, Ybarra86, Schauder87a, Wolodko87, Fong92]

GO Terms:

Molecular Function: GO:0004775 - succinate-CoA ligase (ADP-forming) activity Inferred from experiment [Luo91]

Credits:
Last-Curated ? 30-Oct-2013 by Keseler I , SRI International


Enzymatic reaction of: succinyl-CoA synthetase

Synonyms: succinate thiokinase

EC Number: 6.2.1.5

succinate + ATP + coenzyme A <=> succinyl-CoA + ADP + phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

This reaction is reversible.

Alternative Substrates for succinate: itaconate [Nolte13 ] , (S)-malate [Nolte13 ] , (R)-malate [Nolte13 ]

Alternative Substrates for ATP: GTP [Joyce99 ]

In Pathways: superpathway of glycolysis, pyruvate dehydrogenase, TCA, and glyoxylate bypass , superpathway of glyoxylate bypass and TCA , TCA cycle I (prokaryotic)

Summary:
Initial studies of the enzyme were done in unidentified strains [Kreil64, Nishimura65, Nishimura67] and E. coli (Crookes strain), e.g. [Ramaley67, Sedmak68, Pearson75a, Bridger68, Moffet72, Pearson75, Grinnell69, Lam76, Buttlaire77, Collier78, Collier79, Bild80, Vogel82, Prasad82, Prasad83a, Nishimura83, Prasad83, Wolodko83, Nishimura84, Nishimura84a, Wolodko80a, Williams87, Khan88a, Kelly77].

Low concentrations of ADP stimulate the rate of phosphoenzyme formation [Birney96, Birney97]. An unidentified effector protein inhibits the enzyme; the inhibition is relieved by GDP [Birney97].

The enzyme can utilize some alternative substrates with low efficiency [Nolte13].

Cofactors or Prosthetic Groups: Mg2+

Activators (Unknown Mechanism): ADP [Birney96]

Kinetic Parameters:

Substrate
Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
Citations
(R)-malate
3635.0
1.2
[Nolte13]
(S)-malate
2558.0
1.8
[Nolte13]
GTP
394.0
24.52
[Joyce99]
succinate
250.0
44.73
[Hidber07, BRENDA14]
succinate
141.0
14.3
[Nolte13]
ATP
14.5
[Luo92, BRENDA14]
ATP
70.0
[Hidber07, BRENDA14]
ATP
55.0
19.6
[Nolte13]
coenzyme A
4000.0
[Hidber07, BRENDA14]
coenzyme A
58.0
[Nolte13]
itaconate
475.0
1.5
[Nolte13]


Sequence Features

Feature Class Location Citations Comment
Conserved-Region 9 -> 244
[UniProt09]
UniProt: ATP-grasp;
Nucleotide-Phosphate-Binding-Region 35 -> 108
[UniProt10a]
UniProt: ATP; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 197
[UniProt10a]
UniProt: Magnesium or manganese; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 199
[UniProt10a]
UniProt: Magnesium or manganese; Non-Experimental Qualifier: by similarity;


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b0728 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10981; confirmed by SwissProt match.


References

Arifuzzaman06: Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H (2006). "Large-scale identification of protein-protein interaction of Escherichia coli K-12." Genome Res 16(5);686-91. PMID: 16606699

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bailey99: Bailey DL, Fraser ME, Bridger WA, James MN, Wolodko WT (1999). "A dimeric form of Escherichia coli succinyl-CoA synthetase produced by site-directed mutagenesis." J Mol Biol 285(4);1655-66. PMID: 9917403

Bild80: Bild GS, Janson CA, Boyer PD (1980). "Subunit interaction during catalysis. ATP modulation of catalytic steps in the succinyl-CoA synthetase reaction." J Biol Chem 255(17);8109-15. PMID: 6997289

Birney96: Birney M, Um HD, Klein C (1996). "Novel mechanisms of Escherichia coli succinyl-coenzyme A synthetase regulation." J Bacteriol 178(10);2883-9. PMID: 8631677

Birney97: Birney M, Um H, Klein C (1997). "Multiple levels of regulation of Escherichia coli succinyl-CoA synthetase." Arch Biochem Biophys 347(1);103-12. PMID: 9344470

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

Bridger68: Bridger WA, Millen WA, Boyer PD (1968). "Substrate synergism and phosphoenzyme formation in catalysis by succinyl coenzyme A synthetase." Biochemistry 7(10);3608-16. PMID: 4878702

Bridger71: Bridger WA (1971). "Evidence for two types of subunits in succinyl coenzyme A synthetase." Biochem Biophys Res Commun 42(5);948-54. PMID: 4929931

Bridger87: Bridger WA, Wolodko WT, Henning W, Upton C, Majumdar R, Williams SP (1987). "The subunits of succinyl-coenzyme A synthetase--function and assembly." Biochem Soc Symp 1987;54;103-11. PMID: 3332988

Buck85: Buck D, Spencer ME, Guest JR (1985). "Primary structure of the succinyl-CoA synthetase of Escherichia coli." Biochemistry 24(22);6245-52. PMID: 3002435

Buck86: Buck D, Spencer ME, Guest JR (1986). "Cloning and expression of the succinyl-CoA synthetase genes of Escherichia coli K12." J Gen Microbiol 1986;132 ( Pt 6);1753-62. PMID: 3543212

Buck89: Buck D, Guest JR (1989). "Overexpression and site-directed mutagenesis of the succinyl-CoA synthetase of Escherichia coli and nucleotide sequence of a gene (g30) that is adjacent to the suc operon." Biochem J 1989;260(3);737-47. PMID: 2548486

Buttlaire77: Buttlaire DH, Chon M (1977). "Interactions of phospho- and dephosphosuccinyl coenzyme A synthetase with manganous ion and substrates. Studies of manganese complexes by NMR relaxation rates of water protons." J Biol Chem 252(6);1957-64. PMID: 321448

Collier78: Collier GE, Nishimura JS (1978). "Affinity labeling of succinyl-CoA synthetase from porcine heart and Escherichia coli with oxidized coenzyme A disulfide." J Biol Chem 253(14);4938-43. PMID: 353044

Collier79: Collier GE, Nishimura JS (1979). "Evidence for a second histidine at the active site of succinyl-CoA synthetase from Escherichia coli." J Biol Chem 254(21);10925-30. PMID: 387761

Cunningham98a: Cunningham L, Guest JR (1998). "Transcription and transcript processing in the sdhCDAB-sucABCD operon of Escherichia coli." Microbiology 144 ( Pt 8);2113-23. PMID: 9720032

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Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Fong92: Fong G, Bridger WA (1992). "Folding and assembly of the Escherichia coli succinyl-CoA synthetase heterotetramer without participation of molecular chaperones." Biochemistry 31(24);5661-4. PMID: 1351743

Fraser02: Fraser ME, Joyce MA, Ryan DG, Wolodko WT (2002). "Two glutamate residues, Glu 208 alpha and Glu 197 beta, are crucial for phosphorylation and dephosphorylation of the active-site histidine residue in succinyl-CoA synthetase." Biochemistry 41(2);537-46. PMID: 11781092

Fraser99b: Fraser ME, James MN, Bridger WA, Wolodko WT (1999). "A detailed structural description of Escherichia coli succinyl-CoA synthetase." J Mol Biol 285(4);1633-53. PMID: 9917402

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Grinnell69: Grinnell FL, Nishimura JS (1969). "Succinate thiokinase of Escherichia coli. Purification, phosphorylation of the enzyme, and exchange reactions catalyzed by the enzyme." Biochemistry 8(2);562-8. PMID: 4240087

Grinnell69a: Grinnell FL, Stollar BD, Nishimura JS (1969). "Reversible disaggregation of Escherichia coli succinyl-CoA synthetase." Biochim Biophys Acta 185(2);471-4. PMID: 4980136

Grinnell70: Grinnell F, Nishimura JS (1970). "The inactivation and dissociation of Escherichia coli succinyl-CoA synthetase by sulfhydryl reagents." Biochim Biophys Acta 212(1);150-7. PMID: 5500931

Hidber07: Hidber E, Brownie ER, Hayakawa K, Fraser ME (2007). "Participation of Cys123alpha of Escherichia coli succinyl-CoA synthetase in catalysis." Acta Crystallogr D Biol Crystallogr 63(Pt 8);876-84. PMID: 17642514

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Joyce00: Joyce MA, Fraser ME, James MN, Bridger WA, Wolodko WT (2000). "ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by x-ray crystallography." Biochemistry 39(1);17-25. PMID: 10625475

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Joyce99: Joyce MA, Fraser ME, Brownie ER, James MN, Bridger WA, Wolodko WT (1999). "Probing the nucleotide-binding site of Escherichia coli succinyl-CoA synthetase." Biochemistry 38(22);7273-83. PMID: 10353839

Kelly77: Kelly CJ, Cha S (1977). "Nucleotide specificity of succinate thiokinases from bacteria." Arch Biochem Biophys 178(1);208-17. PMID: 189692

Khan88a: Khan IA, Nishimura JS (1988). "Native-like intermediate on the folding pathway of Escherichia coli succinyl-CoA synthetase." J Biol Chem 263(5);2152-8. PMID: 3276684

Krebs74: Krebs A, Bridger WA (1974). "Some physical parameters of succinyl-coenzyme A synthetase of Escherichia coli." Can J Biochem 52(7);594-8. PMID: 4605130

Kreil64: Kreil G, Boyer PD (1964). "Detection of bound phosphohistidine in E. coli succinate thiokinase." Biochem Biophys Res Commun 16(6);551-5. PMID: 5332854

Lam76: Lam YF, Bridger WA, Kotowycz G (1976). "Nuclear magnetic resonance relaxation time studies on the manganese(II) ion complex with succinyl coenzyme A synthetase from Escherichia coli." Biochemistry 15(21);4742-8. PMID: 788782

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

Leitzmann70: Leitzmann C, Wu JY, Boyer PD (1970). "Subunits, composition, and related properties of succinyl coenzyme A synthetase." Biochemistry 9(11);2338-46. PMID: 4912713

Luo91: Luo GX, Nishimura JS (1991). "Site-directed mutagenesis of Escherichia coli succinyl-CoA synthetase. Histidine 142 alpha is a facilitative catalytic residue." J Biol Chem 266(31);20781-5. PMID: 1939128

Luo92: Luo GX, Nishimura JS (1992). "Adenosine 5'-tetraphosphate is synthesized by the histidine alpha 142----asparagine mutant of Escherichia coli succinyl-CoA synthetase." J Biol Chem 267(14);9516-20. PMID: 1577794

Magnusson86: Magnusson K, Philips MK, Guest JR, Rutberg L (1986). "Nucleotide sequence of the gene for cytochrome b558 of the Bacillus subtilis succinate dehydrogenase complex." J Bacteriol 1986;166(3);1067-71. PMID: 3086287

Mann89: Mann CJ, Hardies SC, Nishimura JS (1989). "Site-directed mutagenesis of Escherichia coli succinyl-CoA synthetase. beta-Cys325 is a nonessential active site residue." J Biol Chem 264(3);1457-60. PMID: 2643599

Mann91: Mann CJ, Mitchell T, Nishimura JS (1991). "Phosphorylation and formation of hybrid enzyme species test the "half of sites" reactivity of Escherichia coli succinyl-CoA synthetase." Biochemistry 30(6);1497-503. PMID: 1993168

MatJan89a: Mat-Jan F, Williams CR, Clark DP (1989). "Anaerobic growth defects resulting from gene fusions affecting succinyl-CoA synthetase in Escherichia coli K12." Mol Gen Genet 215(2);276-80. PMID: 2496297

Miles87b: Miles JS, Guest JR (1987). "Molecular genetic aspects of the citric acid cycle of Escherichia coli." Biochem Soc Symp 54;45-65. PMID: 3332998

Moffet72: Moffet FJ, Wang T, Bridger WA (1972). "Succinyl coenzyme A synthetase of Escherichia coli. Effects of phosphoenzyme formation and of substrate binding on the reactivity and stability of the enzyme." J Biol Chem 247(24);8139-44. PMID: 4565676

Nishimura65: Nishimura JS, Meister A (1965). "Evidence for Succinyl Phosphate as an Enzyme-bound Intermediate in the Reaction Catalyzed by Succinyl Coenzyme A Synthetase." Biochemistry 4(7);1457-1462.

Nishimura67: Nishimura JS (1967). "Formation of succinyl phosphate by reaction of phosphorylated succinic thiokinase with succinate." Biochemistry 6(4);1094-9. PMID: 5340297

Nishimura83: Nishimura JS, Mitchell T, Collier GE, Matula JM, Ball DJ (1983). "Affinity labeling of succinyl-CoA synthetase from Escherichia coli by the 2',3'-dialdehyde derivative of adenosine 5'-diphosphate." Eur J Biochem 136(1);83-7. PMID: 6352264

Nishimura84: Nishimura JS, Mitchell T (1984). "Escherichia coli succinyl coenzyme A synthetase. Inhibition of ATP-stimulated succinate----succinyl coenzyme A exchange at low succinyl coenzyme A concentrations by an ADP trap." J Biol Chem 259(4);2144-8. PMID: 6365903

Nishimura84a: Nishimura JS, Mitchell T (1984). "Adenosine 5'-O-(3-thio)triphosphate, a substrate and potent inhibitor of Escherichia coli succinyl-CoA synthetase. Additional evidence for a cooperative alternating-sites mechanism." J Biol Chem 259(15);9642-5. PMID: 6378911

Nishimura86: Nishimura JS (1986). "Succinyl-CoA synthetase structure-function relationships and other considerations." Adv Enzymol Relat Areas Mol Biol 58;141-72. PMID: 3521216

Nishimura90: Nishimura JS, Mann CJ, Ybarra J, Mitchell T, Horowitz PM (1990). "Intrinsic fluorescence of succinyl-CoA synthetase and four tryptophan mutants. Tryptophan 76 and tryptophan 248 of the beta-subunit are responsive to CoA binding." Biochemistry 29(4);862-5. PMID: 2340278

Nishimura93: Nishimura JS, Ybarra J, Mann CJ, Mitchell T (1993). "Sensitivity of Escherichia coli succinyl-CoA mutants at Trp beta 76 to clostripain and to trypsin. ADP and ATP protect against cleavage by clostripain at Arg beta 80." J Biol Chem 268(18);13717-22. PMID: 8514803

Nolte13: Nolte JC, Schurmann M, Schepers CL, Vogel E, Wubbeler JH, Steinbuchel A (2013). "Novel characteristics of succinate-CoA ligases: conversion of malate to malyl-CoA and CoA-thioester formation of succinate analogues in vitro." Appl Environ Microbiol. PMID: 24141127

OConnorMcCourt85: O'Connor-McCourt MD, Bridger WA (1985). "Chemical modification and hybrid enzyme formation as probes of the active site and subunit interactions in Escherichia coli succinyl-CoA synthetase." Can J Biochem Cell Biol 63(1);57-63. PMID: 3886104

Pearson75: Pearson PH, Bridger WA (1975). "Catalysis of a step of the overall reaction by the alpha subunit of Escherichia coli succinyl coenzyme A synthetase." J Biol Chem 250(21);8524-9. PMID: 1104606

Pearson75a: Pearson PH, Bridger WA (1975). "Isolation of the alpha and beta subunits of Escherichia coli succinyl coenzyme A synthetase and their recombination into active enzyme." J Biol Chem 250(12);4451-5. PMID: 1095571

Prasad82: Prasad AR, Nishimura JS, Horowitz PM (1982). "Fluorescence detection of increased local flexibility induced by coenzyme A in succinyl-coA synthetase from Escherichia coli." Biochemistry 21(21);5142-7. PMID: 6756468

Prasad83: Prasad AR, Ybarra J, Nishimura JS (1983). "Chemical modification of Escherichia coli succinyl-CoA synthetase with the adenine nucleotide analogue 5'-p-fluorosulphonylbenzoyladenosine." Biochem J 215(3);513-8. PMID: 6362660

Prasad83a: Prasad AR, Nishimura JS, Horowitz PM (1983). "A study of the quenching of the intrinsic fluorescence of succinyl-CoA synthetase from Escherichia coli by acrylamide, iodide, and coenzyme A." Biochemistry 22(18);4272-5. PMID: 6354251

Ramaley67: Ramaley RF, Bridger WA, Moyer RW, Boyer PD (1967). "The preparation, properties, and reactions of succinyl coenzyme A synthetase and its phosphorylated form." J Biol Chem 242(19);4287-98. PMID: 4863737

Schauder87a: Schauder B, Blocker H, Frank R, McCarthy JE (1987). "Inducible expression vectors incorporating the Escherichia coli atpE translational initiation region." Gene 52(2-3);279-83. PMID: 3038690

Sedmak68: Sedmak J, Ramaley R (1968). "Identification of succinyl-CoA synthetase as the major phosphorylated protein formed from ATP in Escherichia coli extracts." Biochim Biophys Acta 170(2);440-2. PMID: 4885687

Stancik02: Stancik LM, Stancik DM, Schmidt B, Barnhart DM, Yoncheva YN, Slonczewski JL (2002). "pH-dependent expression of periplasmic proteins and amino acid catabolism in Escherichia coli." J Bacteriol 184(15);4246-58. PMID: 12107143

Thomas74: Thomas EL (1974). "Studies on the metabolism of ATP by isolated bacterial membranes: role of succinyl CoA synthetase in diglyceride kinase activity." Arch Biochem Biophys 163(2);530-6. PMID: 4370406

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Veit07: Veit A, Polen T, Wendisch VF (2007). "Global gene expression analysis of glucose overflow metabolism in Escherichia coli and reduction of aerobic acetate formation." Appl Microbiol Biotechnol 74(2);406-21. PMID: 17273855

Vogel82: Vogel HJ, Bridger WA, Sykes BD (1982). "Frequency-dependent phosphorus-31 nuclear magnetic resonance studies of the phosphohistidine residue to succinyl-CoA synthetase and the phosphoserine residue of glycogen phosphorylase a." Biochemistry 21(6);1126-32. PMID: 6803832

Williams87: Williams SP, Bridger WA (1987). "Positional oxygen isotope exchange as a probe for the mechanism of catalysis by Escherichia coli succinyl coenzyme A synthetase." Biochemistry 26(14);4483-7. PMID: 3311148

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Other References Related to Gene Regulation

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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