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Escherichia coli K-12 substr. MG1655 Enzyme: transaldolase



Gene: talB Accession Numbers: EG11556 (EcoCyc), b0008, ECK0008

Synonyms: yaaK

Regulation Summary Diagram: ?

Subunit composition of transaldolase = [TalB]2
         transaldolase B = TalB

Summary:
Transaldolase B is an enzyme of the non-oxidative branch of the pentose phosphate pathway. Along with transketolase, transaldolase creates a reversible link between the pentose phosphate pathway and glycolysis. It catalyzes the interconversion of glyceraldehyde-3-phosphate and sedoheptulose-7-phosphate to fructose-6-phosphate and erythrose-4-phosphate. The reversibility of this reaction and carbon flux through the pentose phosphate pathway has been addressed both experimentally (summarized in [Katz67]) and theoretically [Katz67, Follstad98, Kleijn05].

There are two closely related transaldolases in E. coli, encoded by talA and talB. Only transaldolase B has been biochemically characterized. TalB is a dimer in solution [Sprenger95a] and in the crystal structure [Jia96]. Mutation of the R300 residue leads to the formation of catalytically active monomers [Schorken98]. Catalytically important active site residues have been identified by site-directed mutagenesis [Schorken01].

Crystal structures of transaldolase B have been determined, confirming the presence of a Schiff-base intermediate at the active site and leading to a proposed reaction mechanism [Jia96, Jia97, Schorken01].

A talB null mutant has no growth defect on minimal media with glucose as the carbon source [Schorken01].

TalB: "transaldolase B" [Sprenger95a]

Review: [Samland09]

Citations: [Zhang95]

Locations: cytosol, membrane

Map Position: [8,238 -> 9,191] (0.18 centisomes)
Length: 954 bp / 317 aa

Molecular Weight of Polypeptide: 35.219 kD (from nucleotide sequence), 35 kD (experimental) [Sprenger95a ]

Molecular Weight of Multimer: 70 kD (experimental) [Sprenger95a]

pI: 5.31

Isozyme Sequence Similarity [Comment 1]:

Unification Links: ASAP:ABE-0000027 , CGSC:36818 , EchoBASE:EB1517 , EcoGene:EG11556 , EcoliWiki:b0008 , ModBase:P0A870 , OU-Microarray:b0008 , PortEco:talB , RefSeq:NP_414549 , RegulonDB:EG11556

Relationship Links: PDB:Structure:1I2N , PDB:Structure:1I2O , PDB:Structure:1I2P , PDB:Structure:1I2Q , PDB:Structure:1I2R , PDB:Structure:1ONR , PDB:Structure:1UCW , Pfam:IN-FAMILY:PF00923

In Paralogous Gene Group: 2 (3 members)

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0009052 - pentose-phosphate shunt, non-oxidative branch Inferred from experiment [Schorken01]
GO:0005975 - carbohydrate metabolic process Inferred by computational analysis [GOA01]
GO:0006098 - pentose-phosphate shunt Inferred by computational analysis [UniProtGOA12, UniProtGOA11, GOA06, GOA01]
Molecular Function: GO:0004801 - sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, GOA01, Sprenger95a]
GO:0016744 - transferase activity, transferring aldehyde or ketonic groups Inferred from experiment [Schorken98]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05, Lasserre06]
GO:0016020 - membrane Inferred from experiment [Lasserre06]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA06, GOA01]

MultiFun Terms: metabolism central intermediary metabolism non-oxidative branch, pentose pathway

Essentiality data for talB knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 2]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 3]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 4]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 3]
Yes [Feist07, Comment 5]

Credits:
Last-Curated ? 06-Oct-2006 by Keseler I , SRI International


Enzymatic reaction of: transaldolase

Synonyms: dehydroxyacetonetransferase, glycerone transferase, sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase

EC Number: 2.2.1.2

D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate <=> β-D-fructofuranose 6-phosphate + D-erythrose 4-phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

This reaction is reversible.

Alternative Substrates [Comment 6]:

In Pathways: pentose phosphate pathway , pentose phosphate pathway (non-oxidative branch)

Summary:
The enzyme has very narrow substrate specificity [Sprenger95a].

Kinetic parameters of the wild type and various mutant enzymes have also been published in [Schorken98] and [Schorken01].

The enzyme is inhibited by sugars with the L-configuration at C2.

Inhibitors (Competitive): phosphate [Sprenger95a] , D-arabinose 5-phosphate [Sprenger95a] , L-glyceraldehyde [Sprenger95a]

Inhibitors (Unknown Mechanism): tris [Sprenger95a]

Kinetic Parameters:

Substrate
Km (μM)
Citations
β-D-fructofuranose 6-phosphate
1200.0
[Sprenger95a]
D-glyceraldehyde 3-phosphate
38.0
[Sprenger95a]
D-erythrose 4-phosphate
90.0
[Sprenger95a]
D-sedoheptulose 7-phosphate
285.0
[Sprenger95a]

pH(opt): 8.5-9.5 [Sprenger95a]


Sequence Features

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[UniProt08]
UniProt: Removed;
Chain 2 -> 317
[UniProt08]
UniProt: Transaldolase B;
Active-Site 132
[UniProt08]
Acetylation-Modification 187
[Yu08]
 
Acetylation-Modification 250
[Yu08]
 
Acetylation-Modification 308
[Yu08]
 


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b0008 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11556; 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

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

Follstad98: Follstad BD, Stephanopoulos G (1998). "Effect of reversible reactions on isotope label redistribution--analysis of the pentose phosphate pathway." Eur J Biochem 252(3);360-71. PMID: 9546650

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

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

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

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

Jia96: Jia J, Huang W, Schorken U, Sahm H, Sprenger GA, Lindqvist Y, Schneider G (1996). "Crystal structure of transaldolase B from Escherichia coli suggests a circular permutation of the alpha/beta barrel within the class I aldolase family." Structure 1996;4(6);715-24. PMID: 8805555

Jia97: Jia J, Schorken U, Lindqvist Y, Sprenger GA, Schneider G (1997). "Crystal structure of the reduced Schiff-base intermediate complex of transaldolase B from Escherichia coli: mechanistic implications for class I aldolases." Protein Sci 1997;6(1);119-24. PMID: 9007983

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

Katz67: Katz J, Rognstad R (1967). "The labeling of pentose phosphate from glucose-14C and estimation of the rates of transaldolase, transketolase, the contribution of the pentose cycle, and ribose phosphate synthesis." Biochemistry 6(7);2227-47. PMID: 6049456

Kleijn05: Kleijn RJ, van Winden WA, van Gulik WM, Heijnen JJ (2005). "Revisiting the 13C-label distribution of the non-oxidative branch of the pentose phosphate pathway based upon kinetic and genetic evidence." FEBS J 272(19);4970-82. PMID: 16176270

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

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Samland09: Samland AK, Sprenger GA (2009). "Transaldolase: from biochemistry to human disease." Int J Biochem Cell Biol 41(7);1482-94. PMID: 19401148

Schorken01: Schorken U, Thorell S, Schurmann M, Jia J, Sprenger GA, Schneider G (2001). "Identification of catalytically important residues in the active site of Escherichia coli transaldolase." Eur J Biochem 268(8);2408-15. PMID: 11298760

Schorken98: Schorken U, Jia J, Sahm H, Sprenger GA, Schneider G (1998). "Disruption of Escherichia coli transaldolase into catalytically active monomers: evidence against half-of-the-sites mechanism." FEBS Lett 441(2);247-50. PMID: 9883893

Sprenger95a: Sprenger GA, Schorken U, Sprenger G, Sahm H (1995). "Transaldolase B of Escherichia coli K-12: cloning of its gene, talB, and characterization of the enzyme from recombinant strains." J Bacteriol 1995;177(20);5930-6. PMID: 7592346

UniProt08: UniProt Consortium (2008). "UniProt version 14.6 released on 2008-12-16." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

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

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

Yu08: Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG (2008). "The diversity of lysine-acetylated proteins in Escherichia coli." J Microbiol Biotechnol 18(9);1529-36. PMID: 18852508

Zhang95: Zhang M, Eddy C, Deanda K, Finkelstein M, Picataggio S (1995). "Metabolic engineering of a pentose metabolism pathway in ethanologenic Zymomonas mobilis." Science 267;240-243.

Other References Related to Gene Regulation

Marzan13: Marzan LW, Hasan CM, Shimizu K (2013). "Effect of acidic condition on the metabolic regulation of Escherichia coli and its phoB mutant." Arch Microbiol 195(3);161-71. PMID: 23274360

MendozaVargas09: Mendoza-Vargas A, Olvera L, Olvera M, Grande R, Vega-Alvarado L, Taboada B, Jimenez-Jacinto V, Salgado H, Juarez K, Contreras-Moreira B, Huerta AM, Collado-Vides J, Morett E (2009). "Genome-wide identification of transcription start sites, promoters and transcription factor binding sites in E. coli." PLoS One 4(10);e7526. PMID: 19838305


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 Sun Dec 21, 2014, BIOCYC13B.