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MetaCyc Enzyme: L-fuculose-phosphate aldolase

Gene: fucA Accession Numbers: EG10348 (MetaCyc), b2800, ECK2795

Synonyms: fucC, prd

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of L-fuculose-phosphate aldolase = [FucA]4

Summary:
FucA can function as both an L-fuculose-phosphate aldolase and a D-ribulose-phosphate aldolase, the third enzyme of the L-fucose and D-arabinose degradation pathways, respectively. However, production of FucA is only induced by L-fucose [LeBlanc71a, LeBlanc71].

The substrate specificity of the enzyme was tested with a partially purified preparation from an unnamed E. coli strain [Ozaki90].

Crystal structures of the enzyme and a number of point mutants have been solved. The combination of structural data and enzymatic activity of mutants allowed modelling and refinement of the catalytic mechanism of the enzyme. [Dreyer93, Dreyer96, Dreyer96a, Joerger00a, Joerger00]

The enantiomeric selectivity of the enzyme has been studied [Joerger00a].

A fucAO deletion mutant colonizes the mouse intestine and maintains its population at a lower level than wild type; the accumulation of fuculose-1-phosphate appears to enable the mutant to switch to utilization of ribose for growth [Autieri07].

Locations: cytosol

Map Position: [2,931,063 <- 2,931,710]

Molecular Weight of Polypeptide: 23.775 kD (from nucleotide sequence)

pI: 6.51

Unification Links: ASAP:ABE-0009179 , CGSC:17701 , EchoBASE:EB0344 , EcoGene:EG10348 , EcoliWiki:b2800 , ModBase:P0AB87 , OU-Microarray:b2800 , PortEco:fucA , PR:PRO_000022727 , Protein Model Portal:P0AB87 , RefSeq:NP_417280 , RegulonDB:EG10348 , SMR:P0AB87 , String:511145.b2800 , UniProt:P0AB87

Relationship Links: InterPro:IN-FAMILY:IPR001303 , InterPro:IN-FAMILY:IPR004782 , PDB:Structure:1DZU , PDB:Structure:1DZV , PDB:Structure:1DZW , PDB:Structure:1DZX , PDB:Structure:1DZY , PDB:Structure:1DZZ , PDB:Structure:1E46 , PDB:Structure:1E47 , PDB:Structure:1E48 , PDB:Structure:1E49 , PDB:Structure:1E4A , PDB:Structure:1E4B , PDB:Structure:1E4C , PDB:Structure:1FUA , PDB:Structure:2FUA , PDB:Structure:3FUA , PDB:Structure:4FUA , Pfam:IN-FAMILY:PF00596 , Smart:IN-FAMILY:SM01007

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0019571 - D-arabinose catabolic process Inferred from experiment [LeBlanc71]
GO:0042355 - L-fucose catabolic process Inferred from experiment [LeBlanc71]
GO:0005975 - carbohydrate metabolic process Inferred by computational analysis [UniProtGOA11]
GO:0006004 - fucose metabolic process Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0019317 - fucose catabolic process Inferred by computational analysis [UniProtGOA12]
Molecular Function: GO:0008738 - L-fuculose-phosphate aldolase activity Inferred from experiment Inferred by computational analysis [GOA01a, GOA01, Joerger00a]
GO:0016832 - aldehyde-lyase activity Inferred from experiment [LeBlanc71]
GO:0008270 - zinc ion binding Inferred by computational analysis [GOA01]
GO:0016829 - lyase activity Inferred by computational analysis [UniProtGOA11]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism carbon utilization carbon compounds

Credits:
Created in EcoCyc 19-Oct-2007 by Keseler I , SRI International
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: L-fuculose-phosphate aldolase

Synonyms: L-fuculose-1-phosphate aldolase, L-fuculose-1-phosphate lactaldehyde-lyase

EC Number: 4.1.2.17

L-fuculose 1-phosphate <=> (S)-lactaldehyde + dihydroxyacetone 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 for (S)-lactaldehyde [Ghalambor62a ]: L-glyceraldehyde [Ghalambor62a ] , glycolaldehyde [Ghalambor62a ]

In Pathways: superpathway of fucose and rhamnose degradation , fucose degradation

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

Summary:
This enzyme was first purified from E. coli strain O-111 B4 [Ghalambor62a].

The Ki for phosphoglycolohydroxamate is 3.1 µM [Fessner96].

Cofactors or Prosthetic Groups: Zn2+ [GarciaJunceda95]

Inhibitors (Competitive): phosphoglycolohydroxamate [Dreyer96a, Fessner96]

Kinetic Parameters:

Substrate
Km (μM)
Citations
L-fuculose 1-phosphate
2200.0
[Joerger00a]


Enzymatic reaction of: D-ribulose-phosphate aldolase (L-fuculose-phosphate aldolase)

D-ribulose 1-phosphate <=> glycolaldehyde + dihydroxyacetone 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.

In Pathways: superpathway of pentose and pentitol degradation , D-arabinose degradation I

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

Summary:
The relative rate of the enzymatic activity with glycolaldehyde as the substrate is 59% of that with lactaldehyde [Ozaki90].

Cofactors or Prosthetic Groups: Zn2+ [GarciaJunceda95]

Inhibitors (Unknown Mechanism): phosphoglycolohydroxamate [Dreyer96a, Fessner96]


Sequence Features

Feature Class Location Citations Comment
Metal-Binding-Site 73
[UniProt10]
UniProt: Zinc;
Active-Site 73
[UniProt10a]
UniProt: Proton acceptor; Non-Experimental Qualifier: probably;
Metal-Binding-Site 92
[UniProt10]
UniProt: Zinc;
Metal-Binding-Site 94
[UniProt10]
UniProt: Zinc;
Active-Site 113
[UniProt10a]
UniProt: Proton donor; Non-Experimental Qualifier: probably;
Metal-Binding-Site 155
[UniProt10]
UniProt: Zinc;

History:
10/20/97 Gene b2800 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10348; confirmed by SwissProt match.


References

Autieri07: Autieri SM, Lins JJ, Leatham MP, Laux DC, Conway T, Cohen PS (2007). "L-fucose stimulates utilization of D-ribose by Escherichia coli MG1655 DeltafucAO and E. coli Nissle 1917 DeltafucAO mutants in the mouse intestine and in M9 minimal medium." Infect Immun 75(11);5465-75. PMID: 17709419

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

Dreyer93: Dreyer MK, Schulz GE (1993). "The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli." J Mol Biol 231(3);549-53. PMID: 8515438

Dreyer96: Dreyer MK, Schulz GE (1996). "Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli." Acta Crystallogr D Biol Crystallogr 52(Pt 6);1082-91. PMID: 15299567

Dreyer96a: Dreyer MK, Schulz GE (1996). "Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure." J Mol Biol 259(3);458-66. PMID: 8676381

Fessner96: Fessner W-D, Schneider A, Held H, Sinerius G, Walter C, Hixon M, Schloss JV (1996). "The mechanism of Class II, metal-dependent aldolases." Angew Chem Int Ed Engl 35:2219-2221.

GarciaJunceda95: Garcia-Junceda E, Shen GJ, Sugai T, Wong CH (1995). "A new strategy for the cloning, overexpression and one step purification of three DHAP-dependent aldolases: rhamnulose-1-phosphate aldolase, fuculose-1-phosphate aldolase and tagatose-1,6-diphosphate aldolase." Bioorg Med Chem 3(7);945-53. PMID: 7582972

Ghalambor62a: Ghalambor MH, Heath EC (1962). "The metabolism of L-fucose. II. The enzymatic cleavage of L-fuculose 1-phosphate." J Biol Chem. Aug;237:2427-33. PMID: 13898172

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.

Joerger00: Joerger AC, Mueller-Dieckmann C, Schulz GE (2000). "Structures of l-fuculose-1-phosphate aldolase mutants outlining motions during catalysis." J Mol Biol 303(4);531-43. PMID: 11054289

Joerger00a: Joerger AC, Gosse C, Fessner WD, Schulz GE (2000). "Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis." Biochemistry 39(20);6033-41. PMID: 10821675

LeBlanc71: LeBlanc DJ, Mortlock RP (1971). "Metabolism of D-arabinose: a new pathway in Escherichia coli." J Bacteriol 106(1);90-6. PMID: 4928018

LeBlanc71a: LeBlanc DJ, Mortlock RP (1971). "Metabolism of D-arabinose: origin of a D-ribulokinase activity in Escherichia coli." J Bacteriol 106(1);82-9. PMID: 4323967

Ozaki90: Ozaki A, Toone EJ, von der Osten CH, Sinskey AJ, Whitesides GM (1990). "Overproduction and substrate specificity of a bacterial fuculose-1-phosphate aldolase: A new enzymatic catalyst for stereocontrolled aldol condensation." J Am Chem Soc 112:4970-4971.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

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

UniProtGOA11: 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."


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 Mon Nov 24, 2014, biocyc13.