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MetaCyc Enzyme: 4-hydroxy-2-ketovalerate aldolase

Gene: mhpE Accession Numbers: G6205 (MetaCyc), b0352, ECK0349

Species: Escherichia coli K-12 substr. MG1655

Summary:
4-hydroxy-2-ketopentanoate aldolase (MhpE) is a stereospecific class I aldolase [Pollard98a].

The expression of MhpE is translationally coupled to MhpF, and interaction between the two proteins appears to be required for solubility of MhpE [Lee06a].

E. coli is able to utilize certain aromatic acids as carbon and energy sources. A meta-cleavage pathway involving MhpE is used for the catabolism of 3-phenylpropionate [Burlingame83].

MhpE: "m-hydroxyphenylpropionate"

Locations: cytosol

Map Position: [373,092 -> 374,105]

Molecular Weight of Polypeptide: 36.47 kD (from nucleotide sequence)

pI: 5.6 [Ferrandez97]

Unification Links: ASAP:ABE-0001209 , DIP:DIP-10209N , EchoBASE:EB3077 , EcoGene:EG13292 , EcoliWiki:b0352 , ModBase:P51020 , OU-Microarray:b0352 , PortEco:mhpE , PR:PRO_000023232 , Pride:P51020 , Protein Model Portal:P51020 , RefSeq:NP_414886 , RegulonDB:G6205 , SMR:P51020 , String:511145.b0352 , Swiss-Model:P51020 , UniProt:P51020

Relationship Links: InterPro:IN-FAMILY:IPR000891 , InterPro:IN-FAMILY:IPR012425 , InterPro:IN-FAMILY:IPR013785 , InterPro:IN-FAMILY:IPR017629 , Panther:IN-FAMILY:PTHR10277:SF3 , Pfam:IN-FAMILY:PF00682 , Pfam:IN-FAMILY:PF07836 , ProDom:IN-FAMILY:PD005364 , Prosite:IN-FAMILY:PS50991

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0019380 - 3-phenylpropionate catabolic process Inferred by computational analysis [UniProtGOA12]
GO:0019439 - aromatic compound catabolic process Inferred by computational analysis [UniProtGOA11, GOA06, GOA01]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Lee06a]
GO:0008701 - 4-hydroxy-2-oxovalerate aldolase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, GOA01, Pollard98a]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01]
GO:0016829 - lyase activity Inferred by computational analysis [UniProtGOA11]
GO:0016833 - oxo-acid-lyase activity Inferred by computational analysis [GOA01]
GO:0030145 - manganese ion binding Inferred by computational analysis [GOA06]
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:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: 4-hydroxy-2-ketovalerate aldolase

Synonyms: HKP aldolase, 4-hydroxy-2-keto-pentanoic acid aldolase, HOA, 4-hydroxy-2-oxovalerate aldolase

EC Number: 4.1.3.39

4-hydroxy-2-oxopentanoate <=> acetaldehyde + pyruvate

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. [Pollard98a]

In Pathways: 3-phenylpropionate and 3-(3-hydroxyphenyl)propionate degradation , 2-oxopentenoate degradation

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

Summary:
The enzyme is highly specific for the acetaldehyde acceptor, but will accept α-ketobutyrate or phenylpyruvate as the carbonyl donor instead of pyruvate. The enzyme is able to catalyze the reverse reaction, but the Keq is 17 M, in favor of the forward reaction [Pollard98a].

Citations: [Lee06a]

Kinetic Parameters:

Substrate
Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
Citations
acetaldehyde
62900.0
205.4
[Wang10a, BRENDA14]

pH(opt): 6.25-6.75 [Pollard98a]


Sequence Features

Feature Class Location Citations Comment
Amino-Acid-Site 14
[UniProt11a]
UniProt: Transition state stabilizer; Sequence Annotation Type: site; Non-Experimental Qualifier: by similarity.
Protein-Segment 14 -> 15
[UniProt11]
UniProt: Substrate binding; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 15
[UniProt11]
UniProt: Manganese; Non-Experimental Qualifier: by similarity.
Active-Site 18
[UniProt11a]
UniProt: Proton acceptor; Non-Experimental Qualifier: potential.
Amino-Acid-Sites-That-Bind 168
[UniProt11]
UniProt: Substrate; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 197
[UniProt11]
UniProt: Manganese; via tele nitrogen; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 199
[UniProt11]
UniProt: Manganese; via tele nitrogen; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 288
[UniProt11]
UniProt: Substrate; Non-Experimental Qualifier: by similarity.

History:
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


References

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

Burlingame83: Burlingame R, Chapman PJ (1983). "Catabolism of phenylpropionic acid and its 3-hydroxy derivative by Escherichia coli." J Bacteriol 1983;155(1);113-21. PMID: 6345502

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

Ferrandez97: Ferrandez A, Garcia JL, Diaz E (1997). "Genetic characterization and expression in heterologous hosts of the 3-(3-hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12." J Bacteriol 1997;179(8);2573-81. PMID: 9098055

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."

Lee06a: Lee SJ, Ko JH, Kang HY, Lee Y (2006). "Coupled expression of MhpE aldolase and MhpF dehydrogenase in Escherichia coli." Biochem Biophys Res Commun 346(3);1009-15. PMID: 16782065

Pollard98a: Pollard JR, Rialland D, Bugg TD (1998). "Substrate selectivity and biochemical properties of 4-hydroxy-2-keto-pentanoic acid aldolase from Escherichia coli." Appl Environ Microbiol 1998;64(10);4093-4. PMID: 9758851

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProt11a: UniProt Consortium (2011). "UniProt version 2011-11 released on 2011-11-22 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."

Wang10a: Wang W, Baker P, Seah SY (2010). "Comparison of two metal-dependent pyruvate aldolases related by convergent evolution: substrate specificity, kinetic mechanism, and substrate channeling." Biochemistry 49(17);3774-82. PMID: 20364820


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 Thu Nov 27, 2014, BIOCYC14B.