|Gene:||yghZ||Accession Numbers: G7558 (EcoCyc), b3001, ECK2995|
Synonyms: mgrA, AKR14A1
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).
|Map Position: [3,145,919 -> 3,146,959] (67.8 centisomes)||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:IPR005399 , InterPro:IN-FAMILY:IPR023210 , Panther:IN-FAMILY:PTHR11732 , Panther:IN-FAMILY:PTHR11732:SF14 , PDB:Structure:3N6Q , PDB:Structure:4AST , PDB:Structure:4AUB , Pfam:IN-FAMILY:PF00248
In Paralogous Gene Group: 65 (9 members)
Instance reaction of [an aldehyde + NADP+ + H2O → a carboxylate + NADPH + 2 H+] (22.214.171.124):
Instance reactions of [an alcohol + NADP+ = an aldehyde + NADPH + H+] (126.96.36.199):
|Biological Process:||GO:0006974 - cellular response to DNA damage stimulus
GO:0009438 - methylglyoxal metabolic process [Grant03a]
GO:0055114 - oxidation-reduction process [UniProtGOA11a]
|Molecular Function:||GO:0016616 - oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0016491 - oxidoreductase activity [UniProtGOA11a]
|MultiFun Terms:||cell processes → protection → detoxification|
|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]
Enzymatic reaction of: L-glyceraldehyde 3-phosphate reductase
EC Number: 1.1.1.-
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.
pH(opt): 6.6 [Kalyananda87]
Enzymatic reaction of: methylglyoxal reductase (L-glyceraldehyde 3-phosphate reductase)
EC Number: 1.1.1.-
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.
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
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
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
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