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discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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MetaCyc Enzyme: periplasmic trehalase

Gene: treA Accession Numbers: EG11017 (MetaCyc), b1197, ECK1185

Synonyms: osmA, tre

Species: Escherichia coli K-12 substr. MG1655

Summary:
E. coli contains two trehalases: the periplasmic TreA (discussed here) and the cytoplasmic TreF. Both enzymes catalyze the hydrolysis of trehalose into two molecules of D-glucose.

Crystal structures of the enzyme alone and complexed with inhibitors have been solved [Gibson07, Cardona09].

Expression of periplasmic trehalase is increased under conditions of high osmolarity [Boos87, Repoila91] and during the transition to stationary phase [HenggeAronis91].

treA mutants accumulate extracellular trehalose under osmotic stress conditions [Styrvold91].

Review: [Strom93]

Locations: periplasmic space

Map Position: [1,244,902 <- 1,246,599]

Molecular Weight of Polypeptide: 63.637 kD (from nucleotide sequence), 58.0 kD (experimental) [Boos87 ]

pI: 5.91

Unification Links: ASAP:ABE-0004021 , CGSC:17572 , DIP:DIP-11022N , EchoBASE:EB1010 , EcoGene:EG11017 , EcoliWiki:b1197 , OU-Microarray:b1197 , PortEco:treA , PR:PRO_000024106 , Pride:P13482 , Protein Model Portal:P13482 , RefSeq:NP_415715 , RegulonDB:EG11017 , SMR:P13482 , String:511145.b1197 , UniProt:P13482

Relationship Links: CAZy:IN-FAMILY:GH37 , InterPro:IN-FAMILY:IPR001661 , InterPro:IN-FAMILY:IPR008928 , InterPro:IN-FAMILY:IPR018232 , InterPro:IN-FAMILY:IPR023720 , Panther:IN-FAMILY:PTHR23403 , PDB:Structure:2JF4 , PDB:Structure:2JG0 , PDB:Structure:2JJB , PDB:Structure:2WYN , Pfam:IN-FAMILY:PF01204 , Prints:IN-FAMILY:PR00744 , Prosite:IN-FAMILY:PS00927 , Prosite:IN-FAMILY:PS00928

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0005993 - trehalose catabolic process Inferred from experiment Inferred by computational analysis [GOA01, Gibson07, Boos87]
GO:0006974 - cellular response to DNA damage stimulus Inferred from experiment [Khil02]
GO:0071474 - cellular hyperosmotic response Inferred from experiment Inferred by computational analysis [GOA01, Repoila91]
GO:0005991 - trehalose metabolic process Inferred by computational analysis [GOA06, GOA01]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0004555 - alpha,alpha-trehalase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, GOA01, Gibson07, Boos87]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11]
GO:0016798 - hydrolase activity, acting on glycosyl bonds Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0030288 - outer membrane-bounded periplasmic space Inferred from experiment [Boos87]
GO:0042597 - periplasmic space Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA06, GOA01]

MultiFun Terms: cell processes adaptations osmotic pressure
metabolism central intermediary metabolism misc. glucose metabolism

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: trehalase

Synonyms: α,α-trehalase, α,α-trehalose glucohydrolase

EC Number: 3.2.1.28

α,α-trehalose[periplasmic space] + H2O[periplasmic space] <=> β-D-glucose[periplasmic space] + α-D-glucose[periplasmic space]

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

The reaction is physiologically favored in the direction shown.

In Pathways: trehalose degradation VI (periplasmic)

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Summary:
The enzyme does not hydrolyze maltose, maltooligosaccharides, sucrose or lactose [Boos87].

Inhibitors (Unknown Mechanism): casuarine [Cardona09]

Kinetic Parameters:

Substrate
Km (μM)
Citations
α,α-trehalose
160.0, 310.0, 1500.0
[Uhland00, BRENDA14]
α,α-trehalose
410.0
[Gibson07]

T(opt): 30 °C [TourinhodosSant94]

pH(opt): 6 [BRENDA14, Horlacher96], 5.5 [TourinhodosSant94]


Sequence Features

Feature Class Location Citations Comment
Signal-Sequence 1 -> 30
[Gutierrez89, UniProt11a]
.
Chain 31 -> 565
[UniProt09]
UniProt: Periplasmic trehalase;
Amino-Acid-Sites-That-Bind 152
[UniProt13]
UniProt: Substrate; Non-Experimental Qualifier: probable.
Protein-Segment 159 -> 160
[UniProt13]
UniProt: Substrate binding; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: probable.
Amino-Acid-Sites-That-Bind 196
[UniProt13]
UniProt: Substrate; Non-Experimental Qualifier: probable.
Protein-Segment 205 -> 207
[UniProt13]
UniProt: Substrate binding; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: probable.
Protein-Segment 277 -> 279
[UniProt13]
UniProt: Substrate binding; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: probable.
Amino-Acid-Sites-That-Bind 310
[UniProt13]
UniProt: Substrate; via carbonyl oxygen; Non-Experimental Qualifier: probable.
Active-Site 312
[UniProt13]
UniProt: Proton donor/acceptor; Non-Experimental Qualifier: by similarity.
Active-Site 496
[UniProt13]
UniProt: Proton donor/acceptor; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 511
[UniProt13]
UniProt: Substrate; Non-Experimental Qualifier: probable.

History:
10/20/97 Gene b1197 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11017; confirmed by SwissProt match.


References

Boos87: Boos W, Ehmann U, Bremer E, Middendorf A, Postma P (1987). "Trehalase of Escherichia coli. Mapping and cloning of its structural gene and identification of the enzyme as a periplasmic protein induced under high osmolarity growth conditions." J Biol Chem 1987;262(27);13212-8. PMID: 2820965

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

Cardona09: Cardona F, Parmeggiani C, Faggi E, Bonaccini C, Gratteri P, Sim L, Gloster TM, Roberts S, Davies GJ, Rose DR, Goti A (2009). "Total syntheses of casuarine and its 6-O-alpha-glucoside: complementary inhibition towards glycoside hydrolases of the GH31 and GH37 families." Chemistry 15(7);1627-36. PMID: 19123216

Gibson07: Gibson RP, Gloster TM, Roberts S, Warren RA, Storch de Gracia I, Garcia A, Chiara JL, Davies GJ (2007). "Molecular basis for trehalase inhibition revealed by the structure of trehalase in complex with potent inhibitors." Angew Chem Int Ed Engl 46(22);4115-9. PMID: 17455176

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."

Gutierrez89: Gutierrez C, Ardourel M, Bremer E, Middendorf A, Boos W, Ehmann U (1989). "Analysis and DNA sequence of the osmoregulated treA gene encoding the periplasmic trehalase of Escherichia coli K12." Mol Gen Genet 217(2-3);347-54. PMID: 2671658

HenggeAronis91: Hengge-Aronis R, Klein W, Lange R, Rimmele M, Boos W (1991). "Trehalose synthesis genes are controlled by the putative sigma factor encoded by rpoS and are involved in stationary-phase thermotolerance in Escherichia coli." J Bacteriol 173(24);7918-24. PMID: 1744047

Horlacher96: Horlacher R, Uhland K, Klein W, Ehrmann M, Boos W (1996). "Characterization of a cytoplasmic trehalase of Escherichia coli." J Bacteriol 178(21);6250-7. PMID: 8892826

Khil02: Khil PP, Camerini-Otero RD (2002). "Over 1000 genes are involved in the DNA damage response of Escherichia coli." Mol Microbiol 44(1);89-105. PMID: 11967071

Repoila91: Repoila F, Gutierrez C (1991). "Osmotic induction of the periplasmic trehalase in Escherichia coli K12: characterization of the treA gene promoter." Mol Microbiol 5(3);747-55. PMID: 1710760

Strom93: Strom AR, Kaasen I (1993). "Trehalose metabolism in Escherichia coli: stress protection and stress regulation of gene expression." Mol Microbiol 1993;8(2);205-10. PMID: 8391102

Styrvold91: Styrvold OB, Strom AR (1991). "Synthesis, accumulation, and excretion of trehalose in osmotically stressed Escherichia coli K-12 strains: influence of amber suppressors and function of the periplasmic trehalase." J Bacteriol 173(3);1187-92. PMID: 1825082

TourinhodosSant94: Tourinho-dos-Santos CF, Bachinski N, Paschoalin VM, Paiva CL, Silva JT, Panek AD (1994). "Periplasmic trehalase from Escherichia coli--characterization and immobilization on spherisorb." Braz J Med Biol Res 27(3);627-36. PMID: 8081287

Uhland00: Uhland K, Mondigler M, Spiess C, Prinz W, Ehrmann M (2000). "Determinants of translocation and folding of TreF, a trehalase of Escherichia coli." J Biol Chem 275(31);23439-45. PMID: 10816581

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

UniProt11a: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProt13: UniProt Consortium (2013). "UniProt version 2013-08 released on 2013-08-01 00:00:00." 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."


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sun Dec 21, 2014, BIOCYC13A.