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Escherichia coli K-12 substr. MG1655 Enzyme: serine hydroxymethyltransferase



Gene: glyA Accession Numbers: EG10408 (EcoCyc), b2551, ECK2548

Regulation Summary Diagram: ?

Subunit composition of serine hydroxymethyltransferase = [GlyA]2
         serine hydroxymethyltransferase = GlyA

Summary:
Serine hydroxymethyltransferase (GlyA) converts serine to glycine, transferring a methyl group to tetrahydrofolate, thus forming 5,10-methylene-tetrahydrofolate (5,10-mTHF). 5,10-mTHF is the major source of C1 units in the cell, making GlyA a key enzyme in the biosynthesis of purines, thymidine, methionine, choline and lipids.

The enzyme also catalyzes several side reactions including hydrolysis of 5,10-methenylTHF to 5-formylTHF [Stover90] and the reversible cleavage of 3-hydroxy amino acids (L-threonine, allothreonine, 3-phenylserine) to glycine and an aldehyde [Schirch85, Hopkins86]. D-alanine inactivates the enzyme by reacting with the pyridoxal phosphate prosthetic group to form pyridoxamine phosphate [Schirch85, Hopkins86].

The Thr226 residue within a conserved region of the enzyme appears to be involved in substrate discrimination [Angelaccio92]. The His228 residue plays a role in determining reaction specificity [Stover92]. Lys229 does not appear to play a catalytic role [Schirch93]. Arg363 appears to be the binding site for the carboxyl group of the amino acid substrate [Delle94]. The hydroxyl group of Tyr65 may be involved in the conversion of the active site from a closed to an open conformation [Contestabile00]. Both Tyr55 and Arg235 are required for the transaldimination reaction [Vivoli09].

Studies on refolding of the enzyme indicate that pyridoxal 5'-phosphate (PLP) only binds to the dimeric apoenzyme at the end of the folding pathway [Cai95]. The mechanism of PLP addition has been investigated further. At high concentrations of PLP, a second molecule of PLP can bind at Lys346 [Malerba07]. A conserved hydrophobic contact area is involved in stability of the PLP binding site [Florio09, Florio09a]. Tyr55 is required for correct positioning of the PLP cofactor [Vivoli09].

Crystal structures of wild type and mutant serine hydroxymethyltransferase have been solved [Scarsdale00, Contestabile00, Vivoli09].

glyA mutants can not use glycine as the sole source of nitrogen [Newman76]. A glyA mutant is auxotrophic for glycine [Pizer65]; glyA was later shown to be essential for growth on glycerol minimal medium [Joyce06].

Sequences 3' to the structural gene within the glyA mRNA are required for mRNA stability [Plamann85, Plamann90].

Review: [Schirch05]

Citations: [Shen13, Loscha13, Herrington13, Blank14]

Gene Citations: [Steiert92, Lorenz95]

Locations: cytosol, membrane

Map Position: [2,682,276 <- 2,683,529] (57.81 centisomes)
Length: 1254 bp / 417 aa

Molecular Weight of Polypeptide: 45.317 kD (from nucleotide sequence), 46.5 kD (experimental) [Plamann83 ]

Molecular Weight of Multimer: 96 kD (experimental) [Schirch85]

pI: 6.41

Unification Links: ASAP:ABE-0008389 , CGSC:675 , DIP:DIP-36205N , EchoBASE:EB0403 , EcoGene:EG10408 , EcoliWiki:b2551 , Entrez-gene:947022 , Mint:MINT-7293373 , ModBase:P0A825 , OU-Microarray:b2551 , PortEco:glyA , PR:PRO_000022816 , Pride:P0A825 , Protein Model Portal:P0A825 , RefSeq:NP_417046 , RegulonDB:EG10408 , SMR:P0A825 , String:511145.b2551 , UniProt:P0A825

Relationship Links: InterPro:IN-FAMILY:IPR001085 , InterPro:IN-FAMILY:IPR015421 , InterPro:IN-FAMILY:IPR015422 , InterPro:IN-FAMILY:IPR015424 , InterPro:IN-FAMILY:IPR019798 , Panther:IN-FAMILY:PTHR11680 , PDB:Structure:1DFO , PDB:Structure:1EQB , PDB:Structure:3G8M , Pfam:IN-FAMILY:PF00464 , Prosite:IN-FAMILY:PS00096

Gene-Reaction Schematic: ?

Instance reaction of [DL-allothreonine ↔ acetaldehyde + glycine] (4.1.2.-):
i1: L-allo-threonine ↔ glycine + acetaldehyde (4.1.2.48/4.1.2.49)

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006546 - glycine catabolic process Inferred from experiment [Newman76]
GO:0006565 - L-serine catabolic process Inferred from experiment [Schirch85]
GO:0019264 - glycine biosynthetic process from serine Inferred from experiment Inferred by computational analysis [GOA06, Pizer65, Schirch85]
GO:0006544 - glycine metabolic process Inferred by computational analysis [GOA01a]
GO:0006545 - glycine biosynthetic process Inferred by computational analysis [UniProtGOA12]
GO:0006563 - L-serine metabolic process Inferred by computational analysis [GOA01a]
GO:0006730 - one-carbon metabolic process Inferred by computational analysis [UniProtGOA11a, GOA06]
GO:0008652 - cellular amino acid biosynthetic process Inferred by computational analysis [UniProtGOA11a]
GO:0035999 - tetrahydrofolate interconversion Inferred by computational analysis [UniProtGOA12]
Molecular Function: GO:0004372 - glycine hydroxymethyltransferase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, Schirch85, Plamann83]
GO:0005515 - protein binding Inferred from experiment [Zheng11]
GO:0008270 - zinc ion binding Inferred from experiment [Katayama02]
GO:0030170 - pyridoxal phosphate binding Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, Malerba07]
GO:0042802 - identical protein binding Inferred from experiment [Florio09a, Lasserre06]
GO:0042803 - protein homodimerization activity Inferred from experiment [Schirch85]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05, Lasserre06]
GO:0016020 - membrane Inferred from experiment [Lasserre06]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06]

MultiFun Terms: metabolism biosynthesis of building blocks amino acids glycine
metabolism carbon utilization amino acids
metabolism central intermediary metabolism formyl-THF biosynthesis

Essentiality data for glyA knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 0.4% glucose No 37 Aerobic 7.2 0.27 No [Patrick07, Comment 2]
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 1]
No [Feist07, Comment 3]

Credits:
Last-Curated ? 24-Aug-2011 by Keseler I , SRI International


Enzymatic reaction of: 5,10-methylenetetrahydrofolate:glycine hydroxymethyltransferase (serine hydroxymethyltransferase)

Synonyms: glycine hydroxymethyltransferase, serine aldolase, serine hydroxymethylase, serine methylase, SHMT, serine transhydroxymethylase, STHM, serine hydroxymethyltransferase

EC Number: 2.1.2.1

L-serine + a tetrahydrofolate <=> glycine + a 5,10-methylene-tetrahydrofolate + H2O

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.

This reaction is reversible.

In Pathways: superpathway of serine and glycine biosynthesis I , glycine biosynthesis I , N10-formyl-tetrahydrofolate biosynthesis , folate polyglutamylation

Summary:
Partial purification and characterization of glycine hydroxymethyltransferase reported in [Mansouri72] used E. coli 113-3 (ATCC 11105), an E. coli W auxotroph.

The Kd for glycine is 850 µM [Schirch85]. The Kd for PLP is 5 nM [Vivoli09].

Cofactors or Prosthetic Groups: pyridoxal 5'-phosphate [Schirch85]

Inhibitors (Competitive): chloride (Kic = 10000µM) [Hopkins86]

Inhibitors (Unknown Mechanism): D-alanine [Hopkins86] , 5,5'-dithio-bis-2-nitrobenzoate [JoshiTope90, Schirch85] , methylmethanethiosulfonate [Schirch85]

Kinetic Parameters:

Substrate
Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
Citations
L-serine
140.0
11.4
[Florio09]
a tetrahydrofolate
7.3
[Florio09]
glycine
250.0
[Hopkins86]


Enzymatic reaction of: 5,10-methenyltetrahydrofolate hydrolase (serine hydroxymethyltransferase)

a 5,10-methenyltetrahydrofolate + H2O <=> an N5-formyl-tetrahydrofolate + 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.

Reversibility of this reaction is unspecified.

Cofactors or Prosthetic Groups: pyridoxal 5'-phosphate [Stover90]

Kinetic Parameters:

Substrate
kcat (sec-1)
Citations
a 5,10-methenyltetrahydrofolate
0.22
[Contestabile00]


Enzymatic reaction of: D-alanine transaminase (serine hydroxymethyltransferase)

D-alanine + pyridoxal 5'-phosphate <=> pyruvate + pyridoxamine 5'-phosphate

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 for D-alanine: L-alanine [Contestabile00 ]

Summary:
The Kd for D-alanine and L-alanine is 30 and 10 mM, respectively [Shostak88].

Kinetic Parameters:

Substrate
Km (μM)
Citations
D-alanine
30000.0
[Stover92]


Enzymatic reaction of: allothreonine acetaldehyde-lyase (glycine-forming) (serine hydroxymethyltransferase)

Synonyms: threonine aldolase, serine hydroxymethyltransferase

EC Number: 4.1.2.-

DL-allothreonine <=> acetaldehyde + glycine

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 for DL-allothreonine: L-threonine [Schirch85 ] , 3-phenylserine [Schirch85 ]

Summary:
The kcat of the reaction is 30 [Hopkins86].

Cofactors or Prosthetic Groups: pyridoxal 5'-phosphate

Kinetic Parameters:

Substrate
Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
Citations
DL-allothreonine
1500.0
[Schirch85]
DL-allothreonine
0.5
[Vivoli09]
L-threonine
12000.0
[Angelaccio92]
acetaldehyde
7100.0
[Makart07]
3-phenylserine
50000.0
[Schirch85]
glycine
25000.0
[Makart07]


Sequence Features

Feature Class Location Citations Comment
Amino-Acid-Sites-That-Bind 35
[UniProt12]
UniProt: Pyridoxal phosphate.
Acetylation-Modification 54
[Zhang09a, UniProt11]
UniProt: N6-acetyllysine.
Mutagenesis-Variant 55
[Vivoli09, UniProt12a]
Alternate sequence: Y → F; UniProt: 50 and 15-fold increase in the affinity for serine and tetrahydrofolate, respectively, and 4-fold decrease in the catalytic efficiency.
Amino-Acid-Sites-That-Bind 55
[UniProt12]
UniProt: Pyridoxal phosphate.
Amino-Acid-Sites-That-Bind 57
[UniProt12]
UniProt: Substrate.
N6-succinyllysine-Modification 62
[Zhang11, UniProt12a]
UniProt: N6-succinyllysine.
Amino-Acid-Sites-That-Bind 64
[UniProt12]
UniProt: Substrate.
Mutagenesis-Variant 65
[Contestabile00, UniProt12a]
Alternate sequence: Y → F; UniProt: Decrease in catalytic activity.
Amino-Acid-Sites-That-Bind 65
[UniProt12]
UniProt: Pyridoxal phosphate.
Mutagenesis-Variant 85
[Florio09, UniProt12a]
Alternate sequence: L → A; UniProt: Alteration of the dimer-monomer equilibrium accompanied by minor changes in the catalytic properties and whitout any significant change of tertiary structure. In the monomeric state; when associated with A-276.
Amino-Acid-Sites-That-Bind 99
[UniProt12]
UniProt: Pyridoxal phosphate.
Amino-Acid-Sites-That-Bind 121
[UniProt12]
UniProt: Substrate.
Protein-Segment 125 -> 127
[UniProt12]
UniProt: Substrate binding; Sequence Annotation Type: region of interest.
Amino-Acid-Sites-That-Bind 175
[UniProt12]
UniProt: Pyridoxal phosphate.
Amino-Acid-Sites-That-Bind 203
[UniProt12]
UniProt: Pyridoxal phosphate.
Mutagenesis-Variant 214
[Fu03, UniProt12a]
Alternate sequence: P → G; UniProt: No significant difference in catalytic efficiency and affinity compared to the wild-type.
Alternate sequence: P → A; UniProt: No significant difference in catalytic efficiency and affinity compared to the wild-type.
Mutagenesis-Variant 216
[Fu03, UniProt12a]
Alternate sequence: P → G; UniProt: Important decrease in affinity and catalytic efficiency. Severely compromised in folding into a catalytically competent enzyme.
Alternate sequence: P → A; UniProt: No significant difference in catalytic efficiency and affinity compared to the wild-type. Alteration in the folding rate.
Mutagenesis-Variant 218
[Fu03, UniProt12a]
Alternate sequence: P → G; UniProt: No significant difference in catalytic efficiency and affinity compared to the wild-type.
Alternate sequence: P → A; UniProt: No significant difference in catalytic efficiency and affinity compared to the wild-type.
Amino-Acid-Sites-That-Bind 228
[UniProt12]
UniProt: Pyridoxal phosphate.
N6-pyridoxal-phosphate-Lys-Modification 229
[UniProt11a]
UniProt: N6-(pyridoxal phosphate)lysine.
Mutagenesis-Variant 235
[Vivoli09, UniProt12a]
Alternate sequence: R → Q; UniProt: 900- and 17-fold increase in the affinity for serine and tetrahydrofolate, respectively, and 30-fold decrease in the catalytic efficiency.
Alternate sequence: R → L; UniProt: 450- and 11-fold increase in the affinity for serine and tetrahydrofolate, respectively, and 60-fold decrease in the catalytic efficiency.
Alternate sequence: R → K; UniProt: 1500- and 20-fold increase in the affinity for serine and tetrahydrofolate, respectively, and 15-fold decrease in the catalytic efficiency.
Amino-Acid-Sites-That-Bind 235
[UniProt12]
UniProt: Pyridoxal phosphate.
N6-succinyllysine-Modification 242
[Zhang11, UniProt12a]
UniProt: N6-succinyllysine.
Amino-Acid-Sites-That-Bind 246
[UniProt12]
UniProt: Substrate.
N6-succinyllysine-Modification 250
[Zhang11, UniProt12a]
UniProt: N6-succinyllysine; alternate.
Acetylation-Modification 250
[Zhang09a, UniProt12a]
UniProt: N6-acetyllysine; alternate.
Mutagenesis-Variant 258
[Fu03, UniProt12a]
Alternate sequence: P → G; UniProt: Important decrease in affinity and catalytic efficiency.
Alternate sequence: P → A; UniProt: Important decrease in affinity and catalytic efficiency. Reduced thermal stability.
Amino-Acid-Sites-That-Bind 263
[UniProt12]
UniProt: Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen.
Mutagenesis-Variant 264
[Fu03, UniProt12a]
Alternate sequence: P → G; UniProt: Important decrease in affinity and catalytic efficiency.
Alternate sequence: P → A; UniProt: Important decrease in affinity and catalytic efficiency.
Mutagenesis-Variant 276
[Florio09, UniProt12a]
Alternate sequence: L → A; UniProt: Alteration of the dimer-monomer equilibrium accompanied by minor changes in the catalytic properties and whitout any significant change of tertiary structure. In the monomeric state; when associated with A-85.
N6-succinyllysine-Modification 277
[Zhang11, UniProt12a]
UniProt: N6-succinyllysine.
Acetylation-Modification 285
[Zhang09a, UniProt11]
UniProt: N6-acetyllysine.
N6-succinyllysine-Modification 293
[Zhang11, UniProt12a]
UniProt: N6-succinyllysine.
N6-succinyllysine-Modification 331
[Zhang11, UniProt12a]
UniProt: N6-succinyllysine.
N6-succinyllysine-Modification 346
[Zhang11, UniProt12a]
UniProt: N6-succinyllysine.
N6-succinyllysine-Modification 354
[Zhang11, UniProt12a]
UniProt: N6-succinyllysine; alternate.
Acetylation-Modification 354
[Zhang09a, UniProt12a]
UniProt: N6-acetyllysine; alternate.
Protein-Segment 355 -> 357
[UniProt12]
UniProt: Substrate binding; Sequence Annotation Type: region of interest.
Mutagenesis-Variant 363
[Delle94, UniProt12a]
Alternate sequence: R → K; UniProt: Exhibits only 0.03% of the catalytic activity of the wild-type and a 15-fold reduction in affinity for glycine and serine.
Alternate sequence: R → A; UniProt: It does not bind serine and glycine and shows no activity with serine as the substrate.
Amino-Acid-Sites-That-Bind 363
[UniProt12]
UniProt: Pyridoxal phosphate.
Mutagenesis-Variant 372
[Delle94, UniProt12a]
Alternate sequence: R → K; UniProt: No significant difference compared to the wild-type.
Alternate sequence: R → A; UniProt: No significant difference compared to the wild-type.
Acetylation-Modification 375
[Zhang09a, UniProt11]
UniProt: N6-acetyllysine.


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b2551 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10408; confirmed by SwissProt match.


References

Angelaccio92: Angelaccio S, Pascarella S, Fattori E, Bossa F, Strong W, Schirch V (1992). "Serine hydroxymethyltransferase: origin of substrate specificity." Biochemistry 31(1);155-62. PMID: 1731867

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

Blank14: Blank D, Wolf L, Ackermann M, Silander OK (2014). "The predictability of molecular evolution during functional innovation." Proc Natl Acad Sci U S A 111(8);3044-9. PMID: 24516157

Cai95: Cai K, Schirch D, Schirch V (1995). "The affinity of pyridoxal 5'-phosphate for folding intermediates of Escherichia coli serine hydroxymethyltransferase." J Biol Chem 270(33);19294-9. PMID: 7642604

Contestabile00: Contestabile R, Angelaccio S, Bossa F, Wright HT, Scarsdale N, Kazanina G, Schirch V (2000). "Role of tyrosine 65 in the mechanism of serine hydroxymethyltransferase." Biochemistry 39(25);7492-500. PMID: 10858298

Delle94: Delle Fratte S, Iurescia S, Angelaccio S, Bossa F, Schirch V (1994). "The function of arginine 363 as the substrate carboxyl-binding site in Escherichia coli serine hydroxymethyltransferase." Eur J Biochem 225(1);395-401. PMID: 7925461

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

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

Fitzpatrick98: Fitzpatrick TB, Malthouse JP (1998). "A substrate-induced change in the stereospecificity of the serine-hydroxymethyltransferase-catalysed exchange of the alpha-protons of amino acids--evidence for a second catalytic site." Eur J Biochem 252(1);113-7. PMID: 9523719

Florio09: Florio R, Chiaraluce R, Consalvi V, Paiardini A, Catacchio B, Bossa F, Contestabile R (2009). "The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia coli serine hydroxymethyltransferase." FEBS J 276(1);132-43. PMID: 19019081

Florio09a: Florio R, Chiaraluce R, Consalvi V, Paiardini A, Catacchio B, Bossa F, Contestabile R (2009). "Structural stability of the cofactor binding site in Escherichia coli serine hydroxymethyltransferase--the role of evolutionarily conserved hydrophobic contacts." FEBS J 276(24);7319-28. PMID: 19909338

Fu03: Fu TF, Boja ES, Safo MK, Schirch V (2003). "Role of proline residues in the folding of serine hydroxymethyltransferase." J Biol Chem 278(33);31088-94. PMID: 12773539

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."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Herrington13: Herrington MB, Sitaras C (2013). "The influence of CsgD on the expression of genes of folate metabolism and hmp in Escherichia coli K-12." Arch Microbiol 195(8);559-69. PMID: 23824318

Hopkins86: Hopkins S, Schirch V (1986). "Properties of a serine hydroxymethyltransferase in which an active site histidine has been changed to an asparagine by site-directed mutagenesis." J Biol Chem 1986;261(7);3363-9. PMID: 3512553

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

JoshiTope90: Joshi-Tope G, Schirch V (1990). "The role of a critical sulfhydryl group in the mechanism of serine hydroxymethyltransferase." Ann N Y Acad Sci 585;339-45. PMID: 2113366

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

Katayama02: Katayama A, Tsujii A, Wada A, Nishino T, Ishihama A (2002). "Systematic search for zinc-binding proteins in Escherichia coli." Eur J Biochem 269(9);2403-13. PMID: 11985624

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Lorenz95: Lorenz E, Stauffer GV (1995). "Characterization of the MetR binding sites for the glyA gene of Escherichia coli." J Bacteriol 1995;177(14);4113-20. PMID: 7608086

Loscha13: Loscha KV, Otting G (2013). "Biosynthetically directed ²H labelling for stereospecific resonance assignments of glycine methylene groups." J Biomol NMR 55(1);97-104. PMID: 23192292

Makart07: Makart S, Bechtold M, Panke S (2007). "Towards preparative asymmetric synthesis of beta-hydroxy-alpha-amino acids: L-allo-threonine formation from glycine and acetaldehyde using recombinant GlyA." J Biotechnol 130(4);402-10. PMID: 17597243

Malerba07: Malerba F, Bellelli A, Giorgi A, Bossa F, Contestabile R (2007). "The mechanism of addition of pyridoxal 5'-phosphate to Escherichia coli apo-serine hydroxymethyltransferase." Biochem J 404(3);477-85. PMID: 17341210

Mansouri72: Mansouri A, Decter JB, Silber R (1972). "Studies on the regulation of one-carbon metabolism. II. Repression-derepression of serine hydroxymethyltransferase by methionine in Escherichia coli 113-3." J Biol Chem 247(2);348-52. PMID: 4550600

Newman76: Newman EB, Batist G, Fraser J, Isenberg S, Weyman P, Kapoor V (1976). "The use of glycine as nitrogen source by Escherichia coli K12." Biochim Biophys Acta 421(1);97-105. PMID: 764875

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

Pizer65: Pizer LI (1965). "Glycine Synthesis and Metabolism in Escherichia coli." J Bacteriol 89;1145-50. PMID: 14276110

Plamann83: Plamann MD, Stauffer GV (1983). "Characterization of the Escherichia coli gene for serine hydroxymethyltransferase." Gene 22(1);9-18. PMID: 6190704

Plamann85: Plamann MD, Stauffer GV (1985). "Characterization of a cis-acting regulatory mutation that maps at the distal end of the Escherichia coli glyA gene." J Bacteriol 161(2);650-4. PMID: 3881406

Plamann90: Plamann MD, Stauffer GV (1990). "Escherichia coli glyA mRNA decay: the role of 3' secondary structure and the effects of the pnp and rnb mutations." Mol Gen Genet 220(2);301-6. PMID: 1691434

Scarsdale00: Scarsdale JN, Radaev S, Kazanina G, Schirch V, Wright HT (2000). "Crystal structure at 2.4 A resolution of E. coli serine hydroxymethyltransferase in complex with glycine substrate and 5-formyl tetrahydrofolate." J Mol Biol 296(1);155-68. PMID: 10656824

Schirch05: Schirch V, Szebenyi DM (2005). "Serine hydroxymethyltransferase revisited." Curr Opin Chem Biol 9(5);482-7. PMID: 16125438

Schirch85: Schirch V, Hopkins S, Villar E, Angelaccio S (1985). "Serine hydroxymethyltransferase from Escherichia coli: purification and properties." J Bacteriol 1985;163(1);1-7. PMID: 3891721

Schirch93: Schirch D, Delle Fratte S, Iurescia S, Angelaccio S, Contestabile R, Bossa F, Schirch V (1993). "Function of the active-site lysine in Escherichia coli serine hydroxymethyltransferase." J Biol Chem 268(31);23132-8. PMID: 8226831

Shen13: Shen T, Rui B, Zhou H, Zhang X, Yi Y, Wen H, Zheng H, Wu J, Shi Y (2013). "Metabolic flux ratio analysis and multi-objective optimization revealed a globally conserved and coordinated metabolic response of E. coli to paraquat-induced oxidative stress." Mol Biosyst 9(1);121-32. PMID: 23128557

Shostak88: Shostak K, Schirch V (1988). "Serine hydroxymethyltransferase: mechanism of the racemization and transamination of D- and L-alanine." Biochemistry 1988;27(21);8007-14. PMID: 3069126

Steiert92: Steiert JG, Kubu C, Stauffer GV (1992). "The PurR binding site in the glyA promoter region of Escherichia coli." FEMS Microbiol Lett 1992;78(2-3);299-304. PMID: 1490614

Stover90: Stover P, Schirch V (1990). "Serine hydroxymethyltransferase catalyzes the hydrolysis of 5,10-methenyltetrahydrofolate to 5-formyltetrahydrofolate." J Biol Chem 265(24);14227-33. PMID: 2201683

Stover92: Stover P, Zamora M, Shostak K, Gautam-Basak M, Schirch V (1992). "Escherichia coli serine hydroxymethyltransferase. The role of histidine 228 in determining reaction specificity." J Biol Chem 267(25);17679-87. PMID: 1517215

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProt11a: UniProt Consortium (2011). "UniProt version 2011-11 released on 2011-11-22 00:00:00." Database.

UniProt12: UniProt Consortium (2012). "UniProt version 2012-02 released on 2012-02-29 00:00:00." Database.

UniProt12a: UniProt Consortium (2012). "UniProt version 2012-09 released on 2012-09-12 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Vivoli09: Vivoli M, Angelucci F, Ilari A, Morea V, Angelaccio S, di Salvo ML, Contestabile R (2009). "Role of a conserved active site cation-pi interaction in Escherichia coli serine hydroxymethyltransferase." Biochemistry 48(50);12034-46. PMID: 19883126

Zhang09a: Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8(2);215-25. PMID: 18723842

Zhang11: Zhang Z, Tan M, Xie Z, Dai L, Chen Y, Zhao Y (2011). "Identification of lysine succinylation as a new post-translational modification." Nat Chem Biol 7(1);58-63. PMID: 21151122

Zhao11: Zhao GH, Li H, Liu W, Zhang WG, Zhang F, Liu Q, Jiao QC (2011). "Preparation of optically active β-hydroxy-α-amino acid by immobilized Escherichia coli cells with serine hydroxymethyl transferase activity." Amino Acids 40(1);215-20. PMID: 20514546

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Other References Related to Gene Regulation

Cho11a: Cho BK, Federowicz SA, Embree M, Park YS, Kim D, Palsson BO (2011). "The PurR regulon in Escherichia coli K-12 MG1655." Nucleic Acids Res 39(15);6456-64. PMID: 21572102

Lorenz96: Lorenz E, Stauffer GV (1996). "Cooperative MetR binding in the Escherichia coli glyA control region." FEMS Microbiol Lett 137(2-3);147-52. PMID: 8998977

Lorenz96a: Lorenz E, Stauffer GV (1996). "MetR-mediated repression of the glyA gene in Escherichia coli." FEMS Microbiol Lett 144(2-3);229-33. PMID: 8900067

Lorenz96b: Lorenz E, Stauffer GV (1996). "RNA polymerase, PurR and MetR interactions at the glyA promoter of Escherichia coli." Microbiology 1996;142 ( Pt 7);1819-24. PMID: 8757744

MembrilloHernan98: Membrillo-Hernandez J, Coopamah MD, Channa A, Hughes MN, Poole RK (1998). "A novel mechanism for upregulation of the Escherichia coli K-12 hmp (flavohaemoglobin) gene by the 'NO releaser', S-nitrosoglutathione: nitrosation of homocysteine and modulation of MetR binding to the glyA-hmp intergenic region." Mol Microbiol 29(4);1101-12. PMID: 9767577

Plamann83b: Plamann MD, Stauffer LT, Urbanowski ML, Stauffer GV (1983). "Complete nucleotide sequence of the E. coli glyA gene." Nucleic Acids Res 1983;11(7);2065-75. PMID: 6300791


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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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