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Escherichia coli K-12 substr. MG1655 Enzyme: o-succinylbenzoate synthase



Gene: menC Accession Numbers: EG11532 (EcoCyc), b2261, ECK2255

Regulation Summary Diagram: ?

Summary:
O-succinylbenzoate synthase catalyzes the formation of the first aromatic intermediate of the menaquinone biosynthetic pathway by dehydration of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate [Sharma93, Palmer99]. MenC belongs to the MLE subfamily of the enolase family of enzymes [Palmer99].

Crystal structures of the ligand-free, mutant enzyme-substrate, and enzyme-product complexes have been solved, and a reaction mechanism has been proposed [Thompson00, Klenchin03]. Site-directed mutagenesis of two proposed active-site lysines, Lys133 and Lys235, yielded catalytically inactive enzymes [Klenchin03].

Review: [Gerlt05]

Gene Citations: [Sharma92, Sharma96]

Locations: cytosol

Map Position: [2,373,022 <- 2,373,984] (51.15 centisomes)
Length: 963 bp / 320 aa

Molecular Weight of Polypeptide: 35.477 kD (from nucleotide sequence)

pI: 5.0

Unification Links: ASAP:ABE-0007473 , CGSC:518 , DIP:DIP-10184N , EchoBASE:EB1494 , EcoGene:EG11532 , EcoliWiki:b2261 , Mint:MINT-1305669 , ModBase:P29208 , OU-Microarray:b2261 , PortEco:menC , PR:PRO_000023202 , Protein Model Portal:P29208 , RefSeq:NP_416764 , RegulonDB:EG11532 , SMR:P29208 , String:511145.b2261 , UniProt:P29208

Relationship Links: InterPro:IN-FAMILY:IPR010196 , InterPro:IN-FAMILY:IPR013342 , PDB:Structure:1FHU , PDB:Structure:1FHV , PDB:Structure:1R6W , PDB:Structure:2OFJ , Pfam:IN-FAMILY:PF01188 , Smart:IN-FAMILY:SM00922

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0009234 - menaquinone biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, UniProtGOA11a, GOA06, GOA01, Guest79]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01]
Molecular Function: GO:0016836 - hydro-lyase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, Palmer99]
GO:0000287 - magnesium ion binding Inferred by computational analysis [GOA01]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01]
GO:0016829 - lyase activity Inferred by computational analysis [UniProtGOA11a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism biosynthesis of building blocks cofactors, small molecule carriers menaquinone, ubiquinone
metabolism energy metabolism, carbon anaerobic respiration

Essentiality data for menC knockouts: ?

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

Credits:
Last-Curated ? 05-Apr-2007 by Keseler I , SRI International


Enzymatic reaction of: o-succinylbenzoate synthase

Synonyms: OSB synthase, 4-(2'-carboxyphenyl)-4-oxybutyric acid synthase

EC Number: 4.2.1.113

(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate <=> 2-succinylbenzoate + H2O

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: superpathway of menaquinol-8 biosynthesis I , superpathway of chorismate metabolism , 1,4-dihydroxy-2-naphthoate biosynthesis I

Cofactors or Prosthetic Groups: Mg2+ [Thompson00]

Kinetic Parameters:

Substrate
Km (μM)
Citations
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
16.0
[Taylor01]

T(opt): 50 °C [BRENDA14, Weische87]

pH(opt): 8.2 [BRENDA14, Weische87]


Sequence Features

Feature Class Location Common Name Citations Comment
Active-Site 133 catalytic base for initial proton abstraction
[Klenchin03]
 
Metal-Binding-Site 161  
[UniProt10]
UniProt: Magnesium;
Sequence-Conflict 176 -> 177  
[Sharma93, UniProt10]
Alternate sequence: KY → missing; UniProt: (in Ref. 1; AAA71917);
Metal-Binding-Site 190  
[UniProt10]
UniProt: Magnesium;
Metal-Binding-Site 213  
[UniProt10]
UniProt: Magnesium;
Active-Site 235  
[UniProt10]
UniProt: Proton acceptor;


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b2261 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11532; confirmed by SwissProt match.


References

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

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

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

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

Gerlt05: Gerlt JA, Babbitt PC, Rayment I (2005). "Divergent evolution in the enolase superfamily: the interplay of mechanism and specificity." Arch Biochem Biophys 433(1);59-70. PMID: 15581566

GOA01: 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."

Guest79: Guest JR (1979). "Anaerobic growth of Escherichia coli K12 with fumarate as terminal electron acceptor. Genetic studies with menaquinone and fluoroacetate-resistant mutants." J Gen Microbiol 115(2);259-71. PMID: 393800

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

Klenchin03: Klenchin VA, Taylor Ringia EA, Gerlt JA, Rayment I (2003). "Evolution of enzymatic activity in the enolase superfamily: structural and mutagenic studies of the mechanism of the reaction catalyzed by o-succinylbenzoate synthase from Escherichia coli." Biochemistry 42(49);14427-33. PMID: 14661953

Meganathan83: Meganathan R, Bentley R (1983). "Thiamine pyrophosphate requirement for o-succinylbenzoic acid synthesis in Escherichia coli and evidence for an intermediate." J Bacteriol 153(2);739-46. PMID: 6337125

Palmer99: Palmer DR, Garrett JB, Sharma V, Meganathan R, Babbitt PC, Gerlt JA (1999). "Unexpected divergence of enzyme function and sequence: "N-acylamino acid racemase" is o-succinylbenzoate synthase." Biochemistry 38(14);4252-8. PMID: 10194342

Sharma92: Sharma V, Suvarna K, Meganathan R, Hudspeth ME (1992). "Menaquinone (vitamin K2) biosynthesis: nucleotide sequence and expression of the menB gene from Escherichia coli." J Bacteriol 1992;174(15);5057-62. PMID: 1629162

Sharma93: Sharma V, Meganathan R, Hudspeth ME (1993). "Menaquinone (vitamin K2) biosynthesis: cloning, nucleotide sequence, and expression of the menC gene from Escherichia coli." J Bacteriol 1993;175(15);4917-21. PMID: 8335646

Sharma96: Sharma V, Hudspeth ME, Meganathan R (1996). "Menaquinone (vitamin K2) biosynthesis: localization and characterization of the menE gene from Escherichia coli." Gene 1996;168(1);43-8. PMID: 8626063

Taylor01: Taylor EA, Palmer DR, Gerlt JA (2001). "The lesser "burden borne" by o-succinylbenzoate synthase: an "easy" reaction involving a carboxylate carbon acid." J Am Chem Soc 123(24);5824-5. PMID: 11403626

Thompson00: Thompson TB, Garrett JB, Taylor EA, Meganathan R, Gerlt JA, Rayment I (2000). "Evolution of enzymatic activity in the enolase superfamily: structure of o-succinylbenzoate synthase from Escherichia coli in complex with Mg2+ and o-succinylbenzoate." Biochemistry 39(35);10662-76. PMID: 10978150

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 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."

Weische87: Weische A, Garvert W, Leistner E (1987). "Biosynthesis of o-succinylbenzoic acid. II: Properties of o-succinylbenzoic acid synthase, an enzyme involved in vitamin K2 biosynthesis." Arch Biochem Biophys 256(1);223-31. PMID: 3300553

Other References Related to Gene Regulation

Zaslaver06: Zaslaver A, Bren A, Ronen M, Itzkovitz S, Kikoin I, Shavit S, Liebermeister W, Surette MG, Alon U (2006). "A comprehensive library of fluorescent transcriptional reporters for Escherichia coli." Nat Methods 3(8);623-8. PMID: 16862137


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Fri Dec 19, 2014, biocyc14.