Escherichia coli K-12 substr. MG1655 Enzyme: D-3-phosphoglycerate dehydrogenase / α-ketoglutarate reductase

Gene: serA Accession Numbers: EG10944 (EcoCyc), b2913, ECK2909

Regulation Summary Diagram: ?

Regulation summary diagram for serA

Subunit composition of D-3-phosphoglycerate dehydrogenase / α-ketoglutarate reductase = [SerA]4

D-3-phosphoglycerate dehydrogenase catalyzes the first committed step in the biosynthesis of L-serine. The enzyme is regulated by allosteric end-product inhibition that shows cooperativity. Inhibition by serine acts primarily through reduction of catalytic velocity and has only a small effect on the Kms of the substrates; SerA is thus classified as a type V allosteric enzyme.

The basis for allosteric and cooperative inhibition by serine has been studied extensively. Occupation of two of the four serine binding sites in the homotetramer results in 85% inhibition of activity [Grant96]. Further binding of serine shows negative cooperativity [Grant99a]. Phosphate is able to reduce the site-to-site cooperative effects on serine binding [Grant99b]; the effect was mainly due to the presence of intrinsically bound NADH [Grant02]. A Trp139Gly mutation results in a homodimeric enzyme that has lost cooperativity in serine binding and allosteric inhibition [Grant00]. Site-directed mutagenesis of residues within the effector binding site, the regulatory interface between subunits, and a flexible hinge region support a model where movement of adjacent domains is involved in inhibition of the enzymatic activity [AlRabiee96, Grant98, Grant01, Grant00a]. Transient kinetic analysis showed that the cooperativity of inhibition of catalytic activity results from a conformational change due to serine binding [Grant11]. An enzyme missing the regulatory domain is no longer inhibited by serine, but other kinetic parameters remain the same [Bell02]. Hybrid tetramers provided further insight into the mechanism of allosteric inhibition [Grant03, Grant04].

Site-directed mutagenesis has allowed the identification of residues within the active site that contribute to substrate binding and catalysis [Grant99]. Mutations in the hinge region between the substrate and nucleotide binding domains affect the kcat of the enzyme; certain mutations uncouple serine binding and catalytic inhibition [Grant01a].

Extensive site-directed mutagenesis and structural studies have contributed to a detailed view of the interactions between allosteric regulation, cooperativity and catalytic activity [Grant05, Dey07]. Further insight into the catalytic pathway was provided by stopped-flow kinetic analysis, indicating that the rate-limiting step in both catalytic directions is a conformational change of the enzyme [Burton08]. Serine binding appears to lead to the formation of a dead-end quaternary complex between the enzyme, coenzyme, substrate, and effector that eliminates the conformational change subsequent to substrate binding [Burton09].

The enzyme has been shown to also have an α-ketoglutarate reductase activity, producing 2-hydroxyglutarate. While the metabolic role of this reaction is not yet known, it is thought that it may play a role in regulating serine biosynthesis and in recycling NADH back to NAD+, especially during anaerobiosis [Zhao96].

Crystal structures of the wild type enzyme and various mutants have been solved [Schuller95, Bell04, Thompson05, Dey07]. The structure showed that each subunit of the homotetramer consists of three distinct domains, a nucleotide binding domain, a substrate binding domain, and a regulatory/serine binding domain [Schuller95].

serA is essential for growth on glycerol minimal medium; the growth defect can be rescued by addition of serine [Joyce06, Ravnikar87, Umbarger63].

Reviews: [Grant12, Grant06, Liberles05]

Citations: [Tobey86, Kim13]

Gene Citations: [Tobey86, Tuan90, Calvo94]

Locations: cytosol

Map Position: [3,055,200 <- 3,056,432] (65.85 centisomes, 237°)
Length: 1233 bp / 410 aa

Molecular Weight of Polypeptide: 44.176 kD (from nucleotide sequence), 40 kD (experimental) [Schuller89 ]

Molecular Weight of Multimer: 163 kD (experimental) [Rosenbloom68]

pI: 6.29

Unification Links: ASAP:ABE-0009561 , CGSC:173 , DIP:DIP-10851N , EchoBASE:EB0937 , EcoGene:EG10944 , EcoliWiki:b2913 , OU-Microarray:b2913 , PortEco:serA , Pride:P0A9T0 , Protein Model Portal:P0A9T0 , RefSeq:NP_417388 , RegulonDB:EG10944 , SMR:P0A9T0 , String:511145.b2913 , UniProt:P0A9T0

Relationship Links: InterPro:IN-FAMILY:IPR002912 , InterPro:IN-FAMILY:IPR006139 , InterPro:IN-FAMILY:IPR006140 , InterPro:IN-FAMILY:IPR016040 , InterPro:IN-FAMILY:IPR029015 , InterPro:IN-FAMILY:IPR029752 , InterPro:IN-FAMILY:IPR029753 , Panther:IN-FAMILY:PTHR10996:SF18 , PDB:Structure:1PSD , PDB:Structure:1SC6 , PDB:Structure:1YBA , PDB:Structure:2P9C , PDB:Structure:2P9E , PDB:Structure:2P9G , PDB:Structure:2PA3 , Pfam:IN-FAMILY:PF00389 , Pfam:IN-FAMILY:PF01842 , Pfam:IN-FAMILY:PF02826 , Prosite:IN-FAMILY:PS00065 , Prosite:IN-FAMILY:PS00670 , Prosite:IN-FAMILY:PS00671 , Prosite:IN-FAMILY:PS51671

In Paralogous Gene Group: 244 (4 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Genetic Regulation Schematic: ?

Genetic regulation schematic for serA

GO Terms:

Biological Process: GO:0006564 - L-serine biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Joyce06]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
GO:0008652 - cellular amino acid biosynthetic process Inferred by computational analysis [UniProtGOA11a]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0004617 - phosphoglycerate dehydrogenase activity Inferred from experiment Inferred by computational analysis [GOA01, GOA01a, Zhao96]
GO:0042802 - identical protein binding Inferred from experiment [Schuller95]
GO:0047545 - 2-hydroxyglutarate dehydrogenase activity Inferred from experiment [Zhao96]
GO:0070905 - serine binding Inferred from experiment [Grant96]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016597 - amino acid binding Inferred by computational analysis [GOA01a]
GO:0016616 - oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Inferred by computational analysis [GOA01a]
GO:0051287 - NAD binding Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]

MultiFun Terms: metabolism biosynthesis of building blocks amino acids serine

Essentiality data for serA 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 0.4% glucose No 37 Aerobic 7.2 0.27 No [Patrick07, Comment 3]
M9 medium with 1% glycerol No 37 Aerobic 7.2 0.35 No [Joyce06]
MOPS medium with 0.4% glucose Indeterminate 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
No [Feist07, Comment 4]

Last-Curated ? 26-Nov-2013 by Keseler I , SRI International

Enzymatic reaction of: D-3-phosphoglycerate dehydrogenase

Synonyms: 3-phosphoglycerate dehydrogenase, phosphoglycerate dehydrogenase, 3-phosphoglycerate:NAD+ 2-oxidoreductase, PGDH

EC Number:

3-phospho-D-glycerate + NAD+ <=> 3-phospho-hydroxypyruvate + NADH + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

This reaction is reversible. [Burton08]

In Pathways: superpathway of L-serine and glycine biosynthesis I , superpathway of sulfate assimilation and cysteine biosynthesis , L-serine biosynthesis

The E. coli B enzyme was first purified and extensively characterized; e.g. [Sugimoto68, Sugimoto68a, Rosenbloom68, Winicov74, Winicov75].

Cofactor Binding Comment: The enzyme contains four coenzyme-binding sites. [Sugimoto68a]

Inhibitors (Allosteric): glycine [Zhao96, Dubrow77, Sugimoto68a] , L-serine [Winicov75]

Primary Physiological Regulators of Enzyme Activity: L-serine

Kinetic Parameters:

Km (μM)

Enzymatic reaction of: α-ketoglutarate reductase

Synonyms: 2-hydroxyglutaric acid dehydrogenase, 2-oxoglutarate reductase

EC Number: 1.1.1.-

2-hydroxyglutarate + NAD+ <=> 2-oxoglutarate + NADH + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

This reaction is reversible.

Alternative Substrates [Comment 5]:

Both D- and L-2-hydroxyglutarate are substrates/products of the enzyme. The Km for D-2-hydroxyglutarate is 370 µM, while the Km for L-2-hydroxyglutarate is 2.9 mM. Kinetics and inhibitors of this reaction have been studied in detail [Zhao96].

Inhibitors (Allosteric): glycine [Zhao96] , L-serine [Zhao96]

Inhibitors (Competitive): 3-phospho-hydroxypyruvate [Zhao96, Comment 6] , 2-oxoglutarate [Zhao96, Comment 7] , 2-hydroxyglutarate [Zhao96, Comment 8]

Inhibitors (Noncompetitive): 3-phospho-D-glycerate [Zhao96]

Primary Physiological Regulators of Enzyme Activity: L-serine

Kinetic Parameters:

Km (μM)

Sequence Features

Protein sequence of SerA with features indicated

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
Chain 2 -> 410
UniProt: D-3-phosphoglycerate dehydrogenase;
Acetylation-Modification 39
Nucleotide-Phosphate-Binding-Region 161 -> 162
UniProt: NAD; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 181
UniProt: NAD; Non-Experimental Qualifier: by similarity;
Nucleotide-Phosphate-Binding-Region 238 -> 240
UniProt: NAD; Non-Experimental Qualifier: by similarity;
Active-Site 240
Amino-Acid-Sites-That-Bind 264
UniProt: NAD; Non-Experimental Qualifier: by similarity;
Active-Site 269
Active-Site 292
UniProt: Proton donor.
Nucleotide-Phosphate-Binding-Region 292 -> 295
UniProt: NAD; Non-Experimental Qualifier: by similarity;
Conserved-Region 339 -> 410
UniProt: ACT.

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram


10/20/97 Gene b2913 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10944; confirmed by SwissProt match.


AlRabiee96: Al-Rabiee R, Zhang Y, Grant GA (1996). "The mechanism of velocity modulated allosteric regulation in D-3-phosphoglycerate dehydrogenase. Site-directed mutagenesis of effector binding site residues." J Biol Chem 271(38);23235-8. PMID: 8798520

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

Bell02: Bell JK, Pease PJ, Bell JE, Grant GA, Banaszak LJ (2002). "De-regulation of D-3-phosphoglycerate dehydrogenase by domain removal." Eur J Biochem 269(17);4176-84. PMID: 12199695

Bell04: Bell JK, Grant GA, Banaszak LJ (2004). "Multiconformational states in phosphoglycerate dehydrogenase." Biochemistry 43(12);3450-8. PMID: 15035616

Burton08: Burton RL, Hanes JW, Grant GA (2008). "A stopped flow transient kinetic analysis of substrate binding and catalysis in Escherichia coli D-3-phosphoglycerate dehydrogenase." J Biol Chem 283(44);29706-14. PMID: 18776184

Burton09: Burton RL, Chen S, Xu XL, Grant GA (2009). "Transient kinetic analysis of the interaction of L-serine with Escherichia coli D-3-phosphoglycerate dehydrogenase reveals the mechanism of V-type regulation and the order of effector binding." Biochemistry 48(51);12242-51. PMID: 19924905

Calvo94: Calvo JM, Matthews RG (1994). "The leucine-responsive regulatory protein, a global regulator of metabolism in Escherichia coli." Microbiol Rev 58(3);466-90. PMID: 7968922

Dey07: Dey S, Hu Z, Xu XL, Sacchettini JC, Grant GA (2007). "The effect of hinge mutations on effector binding and domain rotation in Escherichia coli D-3-phosphoglycerate dehydrogenase." J Biol Chem 282(25);18418-26. PMID: 17459882

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

Dubrow77: Dubrow R, Pizer LI (1977). "Transient kinetic studies on the allosteric transition of phosphoglycerate dehydrogenase." J Biol Chem 1977;252(5);1527-38. PMID: 320209

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

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Grant00: Grant GA, Xu XL, Hu Z (2000). "Removal of the tryptophan 139 side chain in Escherichia coli D-3-phosphoglycerate dehydrogenase produces a dimeric enzyme without cooperative effects." Arch Biochem Biophys 375(1);171-4. PMID: 10683264

Grant00a: Grant GA, Xu XL, Hu Z (2000). "Role of an interdomain Gly-Gly sequence at the regulatory-substrate domain interface in the regulation of Escherichia coli. D-3-phosphoglycerate dehydrogenase." Biochemistry 39(24);7316-9. PMID: 10852732

Grant01: Grant GA, Hu Z, Xu XL (2001). "Specific interactions at the regulatory domain-substrate binding domain interface influence the cooperativity of inhibition and effector binding in Escherichia coli D-3-phosphoglycerate dehydrogenase." J Biol Chem 276(2);1078-83. PMID: 11050089

Grant01a: Grant GA, Hu Z, Xu XL (2001). "Amino acid residue mutations uncouple cooperative effects in Escherichia coli D-3-phosphoglycerate dehydrogenase." J Biol Chem 276(21);17844-50. PMID: 11278587

Grant02: Grant GA, Hu Z, Xu XL (2002). "Cofactor binding to Escherichia coli D-3-phosphoglycerate dehydrogenase induces multiple conformations which alter effector binding." J Biol Chem 277(42);39548-53. PMID: 12183470

Grant03: Grant GA, Hu Z, Xu XL (2003). "Hybrid tetramers reveal elements of cooperativity in Escherichia coli D-3-phosphoglycerate dehydrogenase." J Biol Chem 278(20);18170-6. PMID: 12644455

Grant04: Grant GA, Xu XL, Hu Z (2004). "Quantitative relationships of site to site interaction in Escherichia coli D-3-phosphoglycerate dehydrogenase revealed by asymmetric hybrid tetramers." J Biol Chem 279(14);13452-60. PMID: 14718528

Grant05: Grant GA, Hu Z, Xu XL (2005). "Identification of amino acid residues contributing to the mechanism of cooperativity in Escherichia coli D-3-phosphoglycerate dehydrogenase." Biochemistry 44(51);16844-52. PMID: 16363798

Grant06: Grant GA (2006). "The ACT domain: a small molecule binding domain and its role as a common regulatory element." J Biol Chem 281(45);33825-9. PMID: 16987805

Grant11: Grant GA (2011). "Transient kinetic analysis of L-serine interaction with Escherichia coli D-3-phosphoglycerate dehydrogenase containing amino acid mutations in the hinge regions." Biochemistry 50(14);2900-6. PMID: 21391703

Grant12: Grant GA (2012). "Contrasting catalytic and allosteric mechanisms for phosphoglycerate dehydrogenases." Arch Biochem Biophys 519(2);175-85. PMID: 22023909

Grant96: Grant GA, Schuller DJ, Banaszak LJ (1996). "A model for the regulation of D-3-phosphoglycerate dehydrogenase, a Vmax-type allosteric enzyme." Protein Sci 5(1);34-41. PMID: 8771194

Grant98: Grant GA, Xu XL (1998). "Probing the regulatory domain interface of D-3-phosphoglycerate dehydrogenase with engineered tryptophan residues." J Biol Chem 273(35);22389-94. PMID: 9712860

Grant99: Grant GA, Kim SJ, Xu XL, Hu Z (1999). "The contribution of adjacent subunits to the active sites of D-3-phosphoglycerate dehydrogenase." J Biol Chem 274(9);5357-61. PMID: 10026144

Grant99a: Grant GA, Xu XL, Hu Z (1999). "The relationship between effector binding and inhibition of activity in D-3-phosphoglycerate dehydrogenase." Protein Sci 8(11);2501-5. PMID: 10595555

Grant99b: Grant GA, Xu XL, Hu Z, Purvis AR (1999). "Phosphate ion partially relieves the cooperativity of effector binding in D-3-phosphoglycerate dehydrogenase without altering the cooperativity of inhibition." Biochemistry 38(50);16548-52. PMID: 10600116

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

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

Kim13: Kim HJ, Hou BK, Lee SG, Kim JS, Lee DW, Lee SJ (2013). "Genome-wide analysis of redox reactions reveals metabolic engineering targets for D-lactate overproduction in Escherichia coli." Metab Eng 18;44-52. PMID: 23563322

Liberles05: Liberles JS, Thorolfsson M, Martinez A (2005). "Allosteric mechanisms in ACT domain containing enzymes involved in amino acid metabolism." Amino Acids 28(1);1-12. PMID: 15662561

Link97: Link AJ, Robison K, Church GM (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18(8);1259-313. PMID: 9298646

Patrick07: Patrick WM, Quandt EM, Swartzlander DB, Matsumura I (2007). "Multicopy suppression underpins metabolic evolvability." Mol Biol Evol 24(12);2716-22. PMID: 17884825

Ravnikar87: Ravnikar PD, Somerville RL (1987). "Genetic characterization of a highly efficient alternate pathway of serine biosynthesis in Escherichia coli." J Bacteriol 169(6);2611-7. PMID: 3108237

Rosenbloom68: Rosenbloom J, Sugimoto E, Pizer LI (1968). "The mechanism of end product inhibition of serine biosynthesis. 3. Physical and chemical properties of phosphoglycerate dehydrogenase." J Biol Chem 243(9);2099-107. PMID: 4296830

Schuller89: Schuller DJ, Fetter CH, Banaszak LJ, Grant GA (1989). "Enhanced expression of the Escherichia coli serA gene in a plasmid vector. Purification, crystallization, and preliminary X-ray data of D-3 phosphoglycerate dehydrogenase." J Biol Chem 264(5);2645-8. PMID: 2644267

Schuller95: Schuller DJ, Grant GA, Banaszak LJ (1995). "The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase." Nat Struct Biol 2(1);69-76. PMID: 7719856

Sugimoto68: Sugimoto E, Pizer LI (1968). "The mechanism of end product inhibition of serine biosynthesis. I. Purification and kinetics of phosphoglycerate dehydrogenase." J Biol Chem 1968;243(9);2081-9. PMID: 4384871

Sugimoto68a: Sugimoto E, Pizer LI (1968). "The mechanism of end product inhibition of serine biosynthesis. II. Optical studies of phosphoglycerate dehydrogenase." J Biol Chem 1968;243(9);2090-8. PMID: 4296829

Thompson05: Thompson JR, Bell JK, Bratt J, Grant GA, Banaszak LJ (2005). "Vmax regulation through domain and subunit changes. The active form of phosphoglycerate dehydrogenase." Biochemistry 44(15);5763-73. PMID: 15823035

Tobey86: Tobey KL, Grant GA (1986). "The nucleotide sequence of the serA gene of Escherichia coli and the amino acid sequence of the encoded protein, D-3-phosphoglycerate dehydrogenase." J Biol Chem 1986;261(26);12179-83. PMID: 3017965

Tuan90: Tuan LR, D'Ari R, Newman EB (1990). "The leucine regulon of Escherichia coli K-12: a mutation in rblA alters expression of L-leucine-dependent metabolic operons." J Bacteriol 172(8);4529-35. PMID: 2165479

Umbarger63: Umbarger HE, Umbarger MA, Siu PML (1963). "Biosynthesis of serine in Escherichia coli and Salmonella typhimurium." J Bacteriol 85:1431-1439. PMID: 14047241

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt13: UniProt Consortium (2013). "UniProt version 2013-08 released on 2013-08-01 00:00:00." Database.

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."

Winicov74: Winicov I, Pizer LI (1974). "The mechanism of end product inhibition of serine biosynthesis. IV. Subunit structure of phosphoglycerate dehydrogenase and steady state kinetic studies of phosphoglycerate oxidation." J Biol Chem 249(5);1348-55. PMID: 4361732

Winicov75: Winicov I (1975). "The mechanism of end product inhibition of serine biosynthesis. V. Mechanism of serim inhibition of phosphoglycerate dehydrogenases." J Biol Chem 250(5);1640-7. PMID: 234462

Yu08: Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG (2008). "The diversity of lysine-acetylated proteins in Escherichia coli." J Microbiol Biotechnol 18(9);1529-36. PMID: 18852508

Zhao96: Zhao G, Winkler ME (1996). "A novel alpha-ketoglutarate reductase activity of the serA-encoded 3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its possible implications for human 2-hydroxyglutaric aciduria." J Bacteriol 1996;178(1);232-9. PMID: 8550422

Other References Related to Gene Regulation

Blauwkamp02: Blauwkamp TA, Ninfa AJ (2002). "Nac-mediated repression of the serA promoter of Escherichia coli." Mol Microbiol 45(2);351-63. PMID: 12123449

Yang02a: Yang L, Lin RT, Newman EB (2002). "Structure of the Lrp-regulated serA promoter of Escherichia coli K-12." Mol Microbiol 2002;43(2);323-33. PMID: 11985712

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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