|Gene:||gpsA||Accession Numbers: EG20091 (MetaCyc), b3608, ECK3598|
Species: Escherichia coli K-12 substr. MG1655
Subunit composition of
glycerol-3-phosphate dehydrogenase, biosynthetic = [GpsA]2
glycerol-3-phosphate dehydrogenase = GpsA
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]|
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
Instance reaction of [sn-glycerol 3-phosphate + NAD(P)+ ← glycerone phosphate + NAD(P)H + H+] (188.8.131.52):
|Biological Process:||GO:0046474 - glycerophospholipid biosynthetic process
[Hsu70, Bell74, Cronan74]
GO:0005975 - carbohydrate metabolic process [GOA01]
GO:0006072 - glycerol-3-phosphate metabolic process [GOA01]
GO:0006629 - lipid metabolic process [UniProtGOA11]
GO:0006650 - glycerophospholipid metabolic process [UniProtGOA12]
GO:0008654 - phospholipid biosynthetic process [UniProtGOA11, GOA06]
GO:0046167 - glycerol-3-phosphate biosynthetic process [GOA06]
GO:0046168 - glycerol-3-phosphate catabolic process [GOA01]
GO:0055114 - oxidation-reduction process [UniProtGOA11, GOA01]
|Molecular Function:||GO:0042803 - protein homodimerization activity
GO:0047952 - glycerol-3-phosphate dehydrogenase [NAD(P)+] activity [GOA06, GOA01a, Cronan74, Edgar78]
GO:0004367 - glycerol-3-phosphate dehydrogenase [NAD+] activity [GOA01a, GOA01]
GO:0016491 - oxidoreductase activity [UniProtGOA11, GOA01]
GO:0016616 - oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GOA01]
GO:0036439 - glycerol-3-phosphate dehydrogenase [NADP+] activity [GOA01a]
GO:0050662 - coenzyme binding [GOA01]
GO:0051287 - NAD binding [GOA01]
|Cellular Component:||GO:0005829 - cytosol
GO:0005737 - cytoplasm [UniProtGOA11a, UniProtGOA11, GOA06, GOA01]
GO:0009331 - glycerol-3-phosphate dehydrogenase complex [GOA01]
|MultiFun Terms:||metabolism → central intermediary metabolism → misc. glycerol metabolism|
|metabolism → metabolism of other compounds → phosphorous metabolism|
Enzymatic reaction of: glycerol-3-phosphate dehydrogenase
Synonyms: sn-glycerol-3-phosphate:NAD(P)+ 2-oxidoreductase, glycerol-3-phosphate-dehydrogenase-[NAD(P)+]
EC Number: 184.108.40.206
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.
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
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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