Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015
Pathway Tools
Intro Tutorial
discounted registration ends Sept 5, 2015

Escherichia coli K-12 substr. MG1655 Enzyme: L-glyceraldehyde 3-phosphate reductase

Gene: yghZ Accession Numbers: G7558 (EcoCyc), b3001, ECK2995

Synonyms: mgrA, AKR14A1

Regulation Summary Diagram: ?

Regulation summary diagram for yghZ

YghZ is an L-glyceraldehyde 3-phosphate (L-GAP) reductase [Desai08]; the enzyme is also able to detoxify methylglyoxal at a low rate [Grant03a, Ko05]. YghZ defines the AKR14 (aldo-keto reductase 14) protein family [Grant03a].

L-GAP is not a natural metabolite and is toxic to E. coli [Tang77]. L-GAP is a substrate of both the glycerol-3-phosphate and hexose phosphate transport systems of E.coli K-12 [Tang77, Guth80]. [Desai08] postulate that the physiological role of YghZ is the detoxification of L-GAP, which may be formed by non-enzymatic racemization of GAP or by an unknown cellular process.

Overexpression of yghZ allows a tpiA mutant to grow slowly on L-lactate as the source of carbon. tpiA mutants lack triosephosphate isomerase (TIM), and are thus unable to grow under conditions where gluconeogenesis is required [Desai08]. The YghZ protein does not possess TIM activity [Desai08]. YghZ overproduction results in decreased sensitivity to methylglyoxal, compared to wild type [Grant03a]. Growth of a yghZ gloA double mutant is inhibited by 0.3 mM methylglyoxal [Ko05].

Expression of yghZ is not increased in response to methylglyoxal [Ko05].

The crystal structure of the E. coli enzyme has been determined and was suggested to be a tetramer [Totir12]. However, others have found that the protein forms an octamer based on gel filtration and electron micoscopy studies [Lapthorn13] (author statement).

Reviews: [Richard08, Lapthorn13]

Map Position: [3,145,919 -> 3,146,959] (67.8 centisomes, 244°)
Length: 1041 bp / 346 aa

Molecular Weight of Polypeptide: 38.832 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0009848 , DIP:DIP-36026N , EchoBASE:EB2831 , EcoGene:EG13010 , EcoliWiki:b3001 , ModBase:Q46851 , OU-Microarray:b3001 , PortEco:yghZ , Pride:Q46851 , Protein Model Portal:Q46851 , RefSeq:NP_417474 , RegulonDB:G7558 , SMR:Q46851 , String:511145.b3001 , UniProt:Q46851

Relationship Links: InterPro:IN-FAMILY:IPR001395 , InterPro:IN-FAMILY:IPR023210 , Panther:IN-FAMILY:PTHR11732 , PDB:Structure:3N6Q , PDB:Structure:4AST , PDB:Structure:4AUB , Pfam:IN-FAMILY:PF00248

In Paralogous Gene Group: 65 (9 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Instance reaction of [an aldehyde + NADP+ + H2O → a carboxylate + NADPH + 2 H+] (
i3: acetaldehyde + NADP+ + H2O → acetate + NADPH + 2 H+ (

Instance reactions of [an alcohol + NADP+ = an aldehyde + NADPH + H+] (
i1: (S)-propane-1,2-diol + NADP+ = (S)-lactaldehyde + NADPH + H+ (1.1.1.-)

i2: (R)-propane-1,2-diol + NADP+ = (R)-lactaldehyde + NADPH + H+ (1.1.1.-)

GO Terms:

Biological Process: GO:0006974 - cellular response to DNA damage stimulus Inferred from experiment [Khil02]
GO:0009438 - methylglyoxal metabolic process Inferred from experiment [Grant03a]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0016616 - oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Inferred from experiment [Desai08]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell processes protection detoxification

Essentiality data for yghZ knockouts: ?

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

Curated 24-Jul-2008 by Keseler I , SRI International
Last-Curated ? 14-Feb-2013 by Fulcher C , SRI International

Enzymatic reaction of: L-glyceraldehyde 3-phosphate reductase

EC Number: 1.1.1.-

L-glyceraldehyde 3-phosphate + NADPH + H+ <=> sn-glycerol 3-phosphate + 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.

Kinetic Parameters:

Km (μM)
L-glyceraldehyde 3-phosphate

pH(opt): 6.6 [Kalyananda87]

Enzymatic reaction of: methylglyoxal reductase (L-glyceraldehyde 3-phosphate reductase)

EC Number: 1.1.1.-

acetol + NADP+ <=> methylglyoxal + NADPH + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the opposite direction.

Alternative Substrates for methylglyoxal: 4-nitrobenzaldehyde [Ko05 ]

In Pathways: superpathway of methylglyoxal degradation , methylglyoxal degradation III

Kinetic Parameters:

Km (μM)

Sequence Features

Protein sequence of L-glyceraldehyde 3-phosphate reductase with features indicated

Feature Class Location Citations Comment
Amino-Acid-Site 61
UniProt: Important for catalysis; Sequence Annotation Type: site.
Amino-Acid-Site 66
UniProt: Important for catalysis; Sequence Annotation Type: site.
Amino-Acid-Site 97
UniProt: Important for catalysis; Sequence Annotation Type: site.
Amino-Acid-Site 138
UniProt: Important for catalysis; Sequence Annotation Type: site.

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


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


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

Desai08: Desai KK, Miller BG (2008). "A metabolic bypass of the triosephosphate isomerase reaction." Biochemistry 47(31);7983-5. PMID: 18620424

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

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

Grant03a: Grant AW, Steel G, Waugh H, Ellis EM (2003). "A novel aldo-keto reductase from Escherichia coli can increase resistance to methylglyoxal toxicity." FEMS Microbiol Lett 218(1);93-9. PMID: 12583903

Guth80: Guth A, Engel R, Tropp BE (1980). "Uptake of glycerol 3-phosphate and some of its analogs by the hexose phosphate transport system of Escherichia coli." J Bacteriol 143(1);538-9. PMID: 6995450

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

Kalyananda87: Kalyananda MK, Engel R, Tropp BE (1987). "Metabolism of L-glyceraldehyde 3-phosphate in Escherichia coli." J Bacteriol 169(6);2488-93. PMID: 3294792

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

Ko05: Ko J, Kim I, Yoo S, Min B, Kim K, Park C (2005). "Conversion of methylglyoxal to acetol by Escherichia coli aldo-keto reductases." J Bacteriol 187(16);5782-9. PMID: 16077126

Lapthorn13: Lapthorn AJ, Zhu X, Ellis EM (2013). "The diversity of microbial aldo/keto reductases from Escherichia coli K12." Chem Biol Interact 202(1-3);168-77. PMID: 23103600

Richard08: Richard JP (2008). "Restoring a metabolic pathway." ACS Chem Biol 3(10);605-7. PMID: 18928248

Tang77: Tang CT, Engel R, Tropp BE (1977). "L-Glyceraldehude 3-phosphate, a bactericidal agent." Antimicrob Agents Chemother 11(1);147-53. PMID: 319747

Totir12: Totir M, Echols N, Nanao M, Gee CL, Moskaleva A, Gradia S, Iavarone AT, Berger JM, May AP, Zubieta C, Alber T (2012). "Macro-to-micro structural proteomics: native source proteins for high-throughput crystallization." PLoS One 7(2);e32498. PMID: 22393408

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." Database.

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 EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Sun Aug 30, 2015, biocyc14.