|Gene:||gpsA||Accession Numbers: EG20091 (EcoCyc), b3608, ECK3598|
Glycerol-3-phosphate dehydrogenase (GpsA) catalyzes the NAD(P)H-dependent reduction of the glycolytic intermediate dihydroxyacetone-phosphate to produce glycerol-3-phosphate, a precursor for the biosynthesis of phospholipids [Hsu70, Bell74, Cronan74, Edgar79].
GpsA activity is strongly inhibited in vitro by glycerol-3-phosphate, and it was shown that this inhibition does not involve dimer association or dissociation. A mutant version of the protein which is resistant to feedback inhibition has been studied [Bell75].
The enzyme is constitutively produced, and is present in the cell in low amounts. It was calculated that on average only about 1000 molecules are present per cell [Edgar78].
GpsA did not show dehydrogenase activity in a high-throughput screen of purified proteins [Kuznetsova05].
|Map Position: [3,780,665 <- 3,781,684] (81.49 centisomes, 293°)||Length: 1020 bp / 339 aa|
Molecular Weight of Polypeptide: 36.362 kD (from nucleotide sequence), 32.5 kD (experimental) [Edgar78 ]
Molecular Weight of Multimer: 49 kD (experimental) [Edgar78]
Unification Links: ASAP:ABE-0011795 , CGSC:663 , DIP:DIP-48003N , EchoBASE:EB4142 , EcoGene:EG20091 , EcoliWiki:b3608 , ModBase:P0A6S7 , OU-Microarray:b3608 , PortEco:gpsA , PR:PRO_000022833 , Pride:P0A6S7 , Protein Model Portal:P0A6S7 , RefSeq:NP_418065 , RegulonDB:EG20091 , SMR:P0A6S7 , String:511145.b3608 , UniProt:P0A6S7
Relationship Links: InterPro:IN-FAMILY:IPR006109 , InterPro:IN-FAMILY:IPR006168 , InterPro:IN-FAMILY:IPR008927 , InterPro:IN-FAMILY:IPR011128 , InterPro:IN-FAMILY:IPR013328 , InterPro:IN-FAMILY:IPR016040 , Panther:IN-FAMILY:PTHR11728 , Pfam:IN-FAMILY:PF01210 , Pfam:IN-FAMILY:PF07479 , Prints:IN-FAMILY:PR00077 , Prosite:IN-FAMILY:PS00957
|Biological Process:||GO:0046474 - glycerophospholipid biosynthetic process
[Hsu70, Bell74, Cronan74]
GO:0005975 - carbohydrate metabolic process [GOA01a]
GO:0006072 - glycerol-3-phosphate metabolic process [GOA01a]
GO:0006629 - lipid metabolic process [UniProtGOA11a]
GO:0006650 - glycerophospholipid metabolic process [UniProtGOA12]
GO:0008654 - phospholipid biosynthetic process [UniProtGOA11a, GOA06]
GO:0046167 - glycerol-3-phosphate biosynthetic process [GOA06]
GO:0046168 - glycerol-3-phosphate catabolic process [GOA01a]
GO:0055114 - oxidation-reduction process [UniProtGOA11a, GOA01a]
|Molecular Function:||GO:0042803 - protein homodimerization activity
GO:0047952 - glycerol-3-phosphate dehydrogenase [NAD(P)+] activity [GOA06, GOA01, Cronan74, Edgar78]
GO:0004367 - glycerol-3-phosphate dehydrogenase [NAD+] activity [GOA01, GOA01a]
GO:0016491 - oxidoreductase activity [UniProtGOA11a, GOA01a]
GO:0016616 - oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GOA01a]
GO:0036439 - glycerol-3-phosphate dehydrogenase [NADP+] activity [GOA01]
GO:0050662 - coenzyme binding [GOA01a]
GO:0051287 - NAD binding [GOA01a]
|Cellular Component:||GO:0005829 - cytosol
GO:0005737 - cytoplasm [UniProtGOA11, UniProtGOA11a, GOA06, GOA01a]
GO:0009331 - glycerol-3-phosphate dehydrogenase complex [GOA01a]
|MultiFun Terms:||metabolism → central intermediary metabolism → misc. glycerol metabolism|
|metabolism → metabolism of other compounds → phosphorous metabolism|
|Growth Medium||Growth?||T (°C)||O2||pH||Osm/L||Growth Observations|
|LB enriched||Yes||37||Aerobic||6.95||Yes [Gerdes03, Comment 1]|
|LB Lennox||No||37||Aerobic||7||No [Baba06, Comment 2]|
Enzymatic reaction of: glycerol-3-phosphate dehydrogenase
Synonyms: sn-glycerol-3-phosphate:NAD(P)+ 2-oxidoreductase, glycerol-3-phosphate-dehydrogenase-[NAD(P)+]
EC Number: 18.104.22.168
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.
The enzyme was initially purified from E. coli B [Kito69].
Glycerol phosphate is a competitive inhibitor with respect to dihydroxyacetone phosphate [Edgar78a].
Cofactor Binding Comment: The coenzyme requirement is not strict. [Lin76]
Primary Physiological Regulators of Enzyme Activity: sn-glycerol 3-phosphate
|Nucleotide-Phosphate-Binding-Region||12 -> 17|
|Protein-Segment||259 -> 260|
10/20/97 Gene b3608 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG20091; confirmed by SwissProt match.
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
Bell74: Bell RM (1974). "Mutants of Escherichia coli defective in membrane phospholipid synthesis: macromolecular synthesis in an sn-glycerol 3-phosphate acyltransferase Km mutant." J Bacteriol 117(3);1065-76. PMID: 4591941
Bell75: Bell RM, Cronan JE (1975). "Mutants of Escherichia coli defective in membrane phospholipid synthesis. Phenotypic suppression of sn-glycerol-3-phosphate acyltransferase Km mutants by loss of feedback inhibition of the biosynthetic sn-glycerol-3-phosphate dehydrogenase." J Biol Chem 250(18);7153-8. PMID: 240817
Clark80a: Clark D, Lightner V, Edgar R, Modrich P, Cronan JE, Bell RM (1980). "Regulation of phospholipid biosynthesis in Escherichia coli. Cloning of the structural gene for the biosynthetic sn-glycerol-3-phosphate dehydrogenase." J Biol Chem 255(2);714-7. PMID: 6985897
Cronan74: Cronan JE, Bell RM (1974). "Mutants of Escherichia coli defective in membrane phospholipid synthesis: mapping of the structural gene for L-glycerol 3-phosphate dehydrogenase." J Bacteriol 118(2);598-605. PMID: 4597451
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
Edgar78a: Edgar JR, Bell RM (1978). "Biosynthesis in Escherichia coli of sn-glycerol 3-phosphate, a precursor of phospholipid. Kinetic characterization of wild type and feedback-resistant forms of the biosynthetic sn-glycerol-3-phosphate dehydrogenase." J Biol Chem 253(18);6354-63. PMID: 28326
Edgar79: Edgar JR, Bell RM (1979). "Biosynthesis in Escherichia coli of sn-glycerol 3-phosphate, a precursor of phospholipid. Palmitoyl-CoA inhibition of the biosynthetic sn-glycerol-3-phosphate dehydrogenase." J Biol Chem 1979;254(4);1016-21. PMID: 368067
Edgar80: Edgar JR, Bell RM (1980). "Biosynthesis in Escherichia coli of sn-glycerol-3-phosphate, a precursor of phospholipid. Further kinetic characterization of wild type and feedback-resistant forms of the biosynthetic sn-glycerol-3-phosphate dehydrogenase." J Biol Chem 255(8);3492-7. PMID: 6767719
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
Kuznetsova05: Kuznetsova E, Proudfoot M, Sanders SA, Reinking J, Savchenko A, Arrowsmith CH, Edwards AM, Yakunin AF (2005). "Enzyme genomics: Application of general enzymatic screens to discover new enzymes." FEMS Microbiol Rev 29(2);263-79. PMID: 15808744
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