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Metabolic Modeling Tutorial
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MetaCyc Enzyme: glyoxylate reductase / hydroxypyruvate reductase

Gene: ghrA Accession Numbers: G6539 (MetaCyc), b1033, ECK1019

Synonyms: ycdW

Species: Escherichia coli K-12 substr. MG1655

Summary:
GhrA is one of two enzymes with glyoxylate reductase activity. GhrA prefers NADPH as the electron donor and also catalyzes reduction of hydroxypyruvate, although at lower catalytic efficiency. In contrast, the ghrB-encoded enzyme prefers hydroxypyruvate as the substrate [Nunez01a].

Expression of ghrA is slightly increased by growth on medium containing hydroxypyruvate [Nunez01a]. ghrA was one of only three genes whose expression changed under all stress conditions tested by [Moen09].

Locations: cytosol, inner membrane

Map Position: [1,097,109 -> 1,098,047]

Molecular Weight of Polypeptide: 35.343 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0003503 , EchoBASE:EB3628 , EcoGene:EG13869 , EcoliWiki:b1033 , ModBase:P75913 , OU-Microarray:b1033 , PortEco:ghrA , PR:PRO_000022769 , Pride:P75913 , Protein Model Portal:P75913 , RefSeq:NP_415551 , RegulonDB:G6539 , SMR:P75913 , String:511145.b1033 , UniProt:P75913

Relationship Links: InterPro:IN-FAMILY:IPR006140 , InterPro:IN-FAMILY:IPR016040 , InterPro:IN-FAMILY:IPR023514 , Pfam:IN-FAMILY:PF02826 , Prosite:IN-FAMILY:PS00065 , Prosite:IN-FAMILY:PS00670 , Prosite:IN-FAMILY:PS00671

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0033554 - cellular response to stress Inferred from experiment [Moen09]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01]
Molecular Function: GO:0016618 - hydroxypyruvate reductase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, GOA01, Nunez01a]
GO:0030267 - glyoxylate reductase (NADP) activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, GOA01, Nunez01a]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]
GO:0051287 - NAD binding Inferred by computational analysis [GOA01]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0005886 - plasma membrane Inferred by computational analysis [GOA06]

MultiFun Terms: metabolism

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


Enzymatic reaction of: hydroxypyruvate reductase

EC Number: 1.1.1.-

hydroxypyruvate + NADPH + H+ <=> D-glycerate + NADP+

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. [Nunez01a]

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

Summary:
Activity with NADH as the electron donor is 10% of that with NADPH [Nunez01a].

It is not known whether the product of this reaction is D-glycerate or L-glycerate [Nunez01a].

Kinetic Parameters:

Substrate
Km (μM)
Citations
hydroxypyruvate
1000.0
[Nunez01a]

pH(opt): 7 [Nunez01a]


Enzymatic reaction of: glyoxylate reductase

Synonyms: glycolate:NADP+ oxidoreductase

EC Number: 1.1.1.79

glyoxylate + NADPH + H+ <=> glycolate + NADP+

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. [Nunez01a]

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

Summary:
Activity with NADH as the electron donor is 10% of that with NADPH [Nunez01a].

Kinetic Parameters:

Substrate
Km (μM)
Citations
glyoxylate
600.0
[Nunez01a]

pH(opt): 7 [Nunez01a]


Sequence Features

Feature Class Location Citations Comment
Active-Site 227
[UniProt10a]
UniProt: Non-Experimental Qualifier: by similarity;
Active-Site 275
[UniProt10a]
UniProt: Proton donor; Non-Experimental Qualifier: by similarity;

History:
Peter D. Karp on Wed Jan 18, 2006:
Gene left-end position adjusted based on analysis performed in the 2005 E. coli annotation update [Riley06 ].
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


References

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

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

Moen09: Moen B, Janbu AO, Langsrud S, Langsrud O, Hobman JL, Constantinidou C, Kohler A, Rudi K (2009). "Global responses of Escherichia coli to adverse conditions determined by microarrays and FT-IR spectroscopy." Can J Microbiol 55(6);714-28. PMID: 19767843

Nunez01a: Nunez MF, Pellicer MT, Badia J, Aguilar J, Baldoma L (2001). "Biochemical characterization of the 2-ketoacid reductases encoded by ycdW and yiaE genes in Escherichia coli." Biochem J 354(Pt 3);707-15. PMID: 11237876

Riley06: Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34(1);1-9. PMID: 16397293

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 the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords 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 Thu Dec 18, 2014, biocyc13.