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MetaCyc Protein: aspartate carbamoyltransferase, regulatory subunit

Gene: pyrI Accession Numbers: EG10811 (MetaCyc), b4244, ECK4239

Species: Escherichia coli K-12 substr. MG1655

Component of: aspartate transcarbamylase (extended summary available)

Subunit composition of aspartate carbamoyltransferase, regulatory subunit = [PyrI]2
         aspartate carbamoyltransferase, PyrI subunit = PyrI

Summary:
The regulatory subunit is catalytically inactive but contains the common binding site for the allosteric effectors CTP and ATP [Neidhardt96]. Zn2+ binding to the regulatory subunit is important for its interaction with the catalytic subunit [Nelbach72].

Citations: [Weber68]

Locations: cytosol

Map Position: [4,469,009 <- 4,469,470]

Molecular Weight of Polypeptide: 17.121 kD (from nucleotide sequence), 17.0 kD (experimental) [Rosenbusch71 ]

Molecular Weight of Multimer: 29.0 kD (experimental) [Rosenbusch71]

pI: 7.44

Unification Links: ASAP:ABE-0013889 , CGSC:323 , DIP:DIP-35088N , EchoBASE:EB0804 , EcoGene:EG10811 , EcoliWiki:b4244 , Mint:MINT-1541364 , OU-Microarray:b4244 , PortEco:pyrI , PR:PRO_000023664 , Pride:P0A7F3 , Protein Model Portal:P0A7F3 , RefSeq:NP_418665 , RegulonDB:EG10811 , SMR:P0A7F3 , String:511145.b4244 , UniProt:P0A7F3

Relationship Links: InterPro:IN-FAMILY:IPR002801 , InterPro:IN-FAMILY:IPR020542 , InterPro:IN-FAMILY:IPR020545 , PDB:Structure:1ACM , PDB:Structure:1AT1 , PDB:Structure:1D09 , PDB:Structure:1EZZ , PDB:Structure:1F1B , PDB:Structure:1I5O , PDB:Structure:1NBE , PDB:Structure:1Q95 , PDB:Structure:1R0B , PDB:Structure:1R0C , PDB:Structure:1RAA , PDB:Structure:1RAB , PDB:Structure:1RAC , PDB:Structure:1RAD , PDB:Structure:1RAE , PDB:Structure:1RAF , PDB:Structure:1RAG , PDB:Structure:1RAH , PDB:Structure:1RAI , PDB:Structure:1SKU , PDB:Structure:1TTH , PDB:Structure:1TU0 , PDB:Structure:1TUG , PDB:Structure:1XJW , PDB:Structure:1ZA1 , PDB:Structure:1ZA2 , PDB:Structure:2A0F , PDB:Structure:2AIR , PDB:Structure:2AT1 , PDB:Structure:2ATC , PDB:Structure:2FZC , PDB:Structure:2FZG , PDB:Structure:2FZK , PDB:Structure:2H3E , PDB:Structure:2HSE , PDB:Structure:2IPO , PDB:Structure:2QG9 , PDB:Structure:2QGF , PDB:Structure:3AT1 , PDB:Structure:3D7S , PDB:Structure:3MPU , PDB:Structure:4AT1 , PDB:Structure:4E2F , PDB:Structure:4F04 , PDB:Structure:4FYV , PDB:Structure:4FYW , PDB:Structure:4FYX , PDB:Structure:4FYY , PDB:Structure:5AT1 , PDB:Structure:6AT1 , PDB:Structure:7AT1 , PDB:Structure:8AT1 , PDB:Structure:8ATC , PDB:Structure:9ATC , Pfam:IN-FAMILY:PF01948 , Pfam:IN-FAMILY:PF02748 , ProDom:IN-FAMILY:PD006194

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0006207 - 'de novo' pyrimidine nucleobase biosynthetic process Inferred by computational analysis [GOA01a]
GO:0006221 - pyrimidine nucleotide biosynthetic process Inferred by computational analysis [UniProtGOA11a, GOA06]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Lasserre06, Stieglitz04, Huang04, Alam04, Macol01, Jin00, Jin99, Huang04a]
GO:0008270 - zinc ion binding Inferred from experiment [Nelbach72]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005737 - cytoplasm Inferred from experiment [Lasserre06]
GO:0005829 - cytosol
GO:0009347 - aspartate carbamoyltransferase complex Inferred by computational analysis [GOA01a]

MultiFun Terms: metabolism biosynthesis of building blocks nucleotides pyrimidine biosynthesis
regulation type of regulation posttranscriptional inhibition / activation of enzymes

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Subunit of: aspartate transcarbamylase

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of aspartate transcarbamylase = [(PyrB)3]2[(PyrI)2]3
         aspartate carbamoyltransferase, catalytic subunit = (PyrB)3 (summary available)
                 aspartate carbamoyltransferase, PyrB subunit = PyrB
         aspartate carbamoyltransferase, regulatory subunit = (PyrI)2 (summary available)
                 aspartate carbamoyltransferase, PyrI subunit = PyrI

Summary:
Aspartate transcarbamylase (ATCase) catalyzes the first reaction unique to the de novo biosynthesis of pyrimidine nucleotides. The enzyme and its mechanism of allosteric regulation has been studied extensively; for details and further references to the primary literature, the reader is referred to the comprehensive reviews cited below.

The ATCase holoenzyme consists of two catalytic trimers (encoded by pyrB) and three regulatory dimers (encoded by pyrI) [Gerhart65, Nowlan85]. Numerous crystal structures of the enzyme have been solved (see below). The three regulatory dimers are located at the interface between the two catalytic trimers. Binding of the inhibitor, CTP, causes tightening of the structure, while binding of the activator, ATP, causes opening of the structure.

ATCase catalyzes carbamoyl aspartate formation by an ordered sequential reaction between aspartate and carbamoyl phosphate, showing cooperativity for the second substrate, aspartate [England94]. Allosteric regulation of the enzyme is achieved by a concerted transition between a low-affinity T state to a high-affinity R state that is induced upon binding of carbamoyl phosphate [Gerhart68, Howlett77, Wang05b].

The structural transitions of E. coli aspartate transcarbamylase have been analyzed by X-ray crystallography for several decades and this approach represents a large body of work in the field. Some of the work following the [Helmstaedt01] review is cited here. Structures of unliganded and liganded enzyme have been solved [Wang05b, Stieglitz05, Stieglitz09]. The structures of mutant enzymes have shown functionally important amino acid residues [Stieglitz05a]. Structural studies of the T-state, R-state, and the T to R state transition have also been published [Huang06b, Heng06, Wang07e, Mendes10, Stieglitz04, Eldo06]. In addition, mutants in the PyrB catalytic subunit have been analyzed crystallographically [Alam04, Mendes10a].

Many biophysical [Herve04, West04, Wang08, Mendes10b], kinetic and modeling [Rabinowitz08, Tolonen11], inhibitor [Eldo07, Coudray09, Coudray09a], and mutant analysis [Macol02, Fetler02] studies have also helped to elucidate the function and regulation of aspartate transcarbamylase.

Reviews: [Kantrowitz88, Schachman88, Kantrowitz90, Helmstaedt01, Kantrowitz12]

Molecular Weight: 300.0 kD (experimental) [Rosenbusch71]

GO Terms:

Molecular Function: GO:0004070 - aspartate carbamoyltransferase activity Inferred from experiment [GERHART62]
GO:0008270 - zinc ion binding Inferred from experiment [Rosenbusch71]
Cellular Component: GO:0009347 - aspartate carbamoyltransferase complex Inferred from experiment [Gerhart65]

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: aspartate transcarbamylase

Synonyms: carbamylaspartotranskinase, ATCase, carbamoyl-phosphate:L-aspartate carbamoyltransferase, aspartate transcarbamoylase, aspartate carbamoyltransferase

EC Number: 2.1.3.2

L-aspartate + carbamoyl-phosphate <=> N-carbamoyl-L-aspartate + phosphate + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

This reaction is reversible.

In Pathways: superpathway of histidine, purine, and pyrimidine biosynthesis , superpathway of pyrimidine deoxyribonucleotides de novo biosynthesis , superpathway of pyrimidine ribonucleotides de novo biosynthesis , UMP biosynthesis

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Summary:
UTP potentiates inhibition by CTP [Wild89, Zhang91, Hoover83]. The inhibitor CTP and the activator ATP do not simply act in inverse ways on the same equilibrium [Van91a].

The enzyme binds Zn2+ tightly, but the ion does not appear to be required for catalytic activity [Rosenbusch71].

Mutant analysis indicated that aspartate and carbamyl phosphate homotropic co-operativity are separable and that CTP inhibition can be partially decoupled from ATP activation [Silver83].

Cofactor Binding Comment: Zinc binding domain interacts with the catalytic subunit; CTP binding domain interacts with an adjacent regulatory subunit. [Monaco78]

Activators (Allosteric): ATP [Ke84, GERHART62]

Inhibitors (Allosteric): CTP [Zhang91, Hoover83, Weitzman66, GERHART62]

Inhibitors (Competitive): succinate [Changeux68, Comment 1] , N-(phosphonacetyl)-L-aspartate [Collins71, Comment 2]

Primary Physiological Regulators of Enzyme Activity: ATP , CTP


Sequence Features

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[Pasquali94, Weber68, Link97, UniProt12a]
UniProt: Removed.
Chain 2 -> 153
[UniProt09]
UniProt: Aspartate carbamoyltransferase regulatory chain;
Metal-Binding-Site 109
[UniProt10]
UniProt: Zinc;
Metal-Binding-Site 114
[UniProt10]
UniProt: Zinc;
Metal-Binding-Site 138
[UniProt10]
UniProt: Zinc;
Metal-Binding-Site 141
[UniProt10]
UniProt: Zinc;

History:
10/20/97 Gene b4244 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10811; confirmed by SwissProt match.


References

Alam04: Alam N, Stieglitz KA, Caban MD, Gourinath S, Tsuruta H, Kantrowitz ER (2004). "240s loop interactions stabilize the T state of Escherichia coli aspartate transcarbamoylase." J Biol Chem 279(22);23302-10. PMID: 15014067

Changeux68: Changeux JP, Gerhart JC, Schachman HK (1968). "Allosteric interactions in aspartate transcarbamylase. I. Binding of specific ligands to the native enzyme and its isolated subunits." Biochemistry 7(2);531-8. PMID: 4868539

Collins71: Collins KD, Stark GR (1971). "Aspartate transcarbamylase. Interaction with the transition state analogue N-(phosphonacetyl)-L-aspartate." J Biol Chem 1971;246(21);6599-605. PMID: 4943676

Coudray09: Coudray L, Pennebaker AF, Montchamp JL (2009). "Synthesis and in vitro evaluation of aspartate transcarbamoylase inhibitors." Bioorg Med Chem 17(22);7680-9. PMID: 19828320

Coudray09a: Coudray L, Kantrowitz ER, Montchamp JL (2009). "Submicromolar phosphinic inhibitors of Escherichia coli aspartate transcarbamoylase." Bioorg Med Chem Lett 19(3);900-2. PMID: 19097895

Eldo06: Eldo J, Cardia JP, O'Day EM, Xia J, Tsuruta H, Kantrowitz ER (2006). "N-phosphonacetyl-L-isoasparagine a potent and specific inhibitor of Escherichia coli aspartate transcarbamoylase." J Med Chem 49(20);5932-8. PMID: 17004708

Eldo07: Eldo J, Heng S, Kantrowitz ER (2007). "Design, synthesis, and bioactivity of novel inhibitors of E. coli aspartate transcarbamoylase." Bioorg Med Chem Lett 17(7);2086-90. PMID: 17336518

England94: England P, Leconte C, Tauc P, Herve G (1994). "Apparent cooperativity for carbamoylphosphate in Escherichia coli aspartate transcarbamoylase only reflects cooperativity for aspartate." Eur J Biochem 222(3);775-80. PMID: 8026491

Fetler02: Fetler L, Tauc P, Baker DP, Macol CP, Kantrowitz ER, Vachette P (2002). "Replacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylase." Protein Sci 11(5);1074-81. PMID: 11967364

GERHART62: GERHART JC, PARDEE AB (1962). "The enzymology of control by feedback inhibition." J Biol Chem 237;891-6. PMID: 13897943

Gerhart65: Gerhart JC, Schachman HK (1965). "Distinct subunits for the regulation and catalytic activity of aspartate transcarbamylase." Biochemistry 4(6);1054-62. PMID: 5320387

Gerhart67: Gerhart JC, Holoubek H (1967). "The purification of aspartate transcarbamylase of Escherichia coli and separation of its protein subunits." J Biol Chem 242(12);2886-92. PMID: 5338508

Gerhart68: Gerhart JC, Schachman HK (1968). "Allosteric interactions in aspartate transcarbamylase. II. Evidence for different conformational states of the protein in the presence and absence of specific ligands." Biochemistry 7(2);538-52. PMID: 4868540

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."

Helmstaedt01: Helmstaedt K, Krappmann S, Braus GH (2001). "Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase." Microbiol Mol Biol Rev 65(3);404-21, table of contents. PMID: 11528003

Helmward89: Helmward Z "Handbook of Enzyme Inhibitors. 2nd, revised and enlarged edition." Weinheim, Federal Republic of Germany ; New York, NY, USA , 1989.

Heng06: Heng S, Stieglitz KA, Eldo J, Xia J, Cardia JP, Kantrowitz ER (2006). "T-state inhibitors of E. coli aspartate transcarbamoylase that prevent the allosteric transition." Biochemistry 45(33);10062-71. PMID: 16906764

Herve04: Herve G, Schmitt B, Serre V (2004). "Cooperativity and high pressure: stabilization of the R conformation of the allosteric aspartate transcarbamylase under the influence of pressure." Cell Mol Biol (Noisy-le-grand) 50(4);347-52. PMID: 15529744

Hoover83: Hoover TA, Roof WD, Foltermann KF, O'Donovan GA, Bencini DA, Wild JR (1983). "Nucleotide sequence of the structural gene (pyrB) that encodes the catalytic polypeptide of aspartate transcarbamoylase of Escherichia coli." Proc Natl Acad Sci U S A 1983;80(9);2462-6. PMID: 6302686

Howlett77: Howlett GJ, Blackburn MN, Compton JG, Schachman HK (1977). "Allosteric regulation of aspartate transcarbamoylase. Analysis of the structural and functional behavior in terms of a two-state model." Biochemistry 16(23);5091-100. PMID: 334257

Huang04: Huang J, Lipscomb WN (2004). "Aspartate transcarbamylase (ATCase) of Escherichia coli: a new crystalline R-state bound to PALA, or to product analogues citrate and phosphate." Biochemistry 43(21);6415-21. PMID: 15157075

Huang04a: Huang J, Lipscomb WN (2004). "Products in the T-state of aspartate transcarbamylase: crystal structure of the phosphate and N-carbamyl-L-aspartate ligated enzyme." Biochemistry 43(21);6422-6. PMID: 15157076

Huang06b: Huang J, Lipscomb WN (2006). "T-state active site of aspartate transcarbamylase: crystal structure of the carbamyl phosphate and L-alanosine ligated enzyme." Biochemistry 45(2);346-52. PMID: 16401065

Jin00: Jin L, Stec B, Kantrowitz ER (2000). "A cis-proline to alanine mutant of E. coli aspartate transcarbamoylase: kinetic studies and three-dimensional crystal structures." Biochemistry 39(27);8058-66. PMID: 10891088

Jin99: Jin L, Stec B, Lipscomb WN, Kantrowitz ER (1999). "Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 A." Proteins 37(4);729-42. PMID: 10651286

Kantrowitz12: Kantrowitz ER (2012). "Allostery and cooperativity in Escherichia coli aspartate transcarbamoylase." Arch Biochem Biophys 519(2);81-90. PMID: 22198283

Kantrowitz88: Kantrowitz ER, Lipscomb WN (1988). "Escherichia coli aspartate transcarbamylase: the relation between structure and function." Science 241(4866);669-74. PMID: 3041592

Kantrowitz90: Kantrowitz ER, Lipscomb WN (1990). "Escherichia coli aspartate transcarbamoylase: the molecular basis for a concerted allosteric transition." Trends Biochem Sci 15(2);53-9. PMID: 2186515

Ke84: Ke HM, Honzatko RB, Lipscomb WN (1984). "Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolution." Proc Natl Acad Sci U S A 1984;81(13);4037-40. PMID: 6377306

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

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

Macol01: Macol CP, Tsuruta H, Stec B, Kantrowitz ER (2001). "Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase." Nat Struct Biol 8(5);423-6. PMID: 11323717

Macol02: Macol CP, Tsuruta H, Kantrowitz ER (2002). "Importance of domain closure for the catalysis and regulation of Escherichia coli aspartate transcarbamoylase." J Biol Chem 277(30);26852-7. PMID: 12016227

Mendes10: Mendes KR, Kantrowitz ER (2010). "The pathway of product release from the R state of aspartate transcarbamoylase." J Mol Biol 401(5);940-8. PMID: 20620149

Mendes10a: Mendes KR, Kantrowitz ER (2010). "A cooperative Escherichia coli aspartate transcarbamoylase without regulatory subunits." Biochemistry 49(35);7694-703. PMID: 20681545

Mendes10b: Mendes KR, Martinez JA, Kantrowitz ER (2010). "Asymmetric allosteric signaling in aspartate transcarbamoylase." ACS Chem Biol 5(5);499-506. PMID: 20210358

Monaco78: Monaco HL, Crawford JL, Lipscomb WN (1978). "Three-dimensional structures of aspartate carbamoyltransferase from Escherichia coli and of its complex with cytidine triphosphate." Proc Natl Acad Sci U S A 1978;75(11);5276-80. PMID: 364472

Neidhardt96: Neidhardt FC, Curtiss III R, Ingraham JL, Lin ECC, Low Jr KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE "Escherichia coli and Salmonella, Cellular and Molecular Biology, Second Edition." American Society for Microbiology, Washington, D.C., 1996.

Nelbach72: Nelbach ME, Pigiet VP, Gerhart JC, Schachman HK (1972). "A role for zinc in the quaternary structure of aspartate transcarbamylase from Escherichia coli." Biochemistry 11(3);315-27. PMID: 4550953

Nowlan85: Nowlan SF, Kantrowitz ER (1985). "Superproduction and rapid purification of Escherichia coli aspartate transcarbamylase and its catalytic subunit under extreme derepression of the pyrimidine pathway." J Biol Chem 1985;260(27);14712-6. PMID: 3902838

Pasquali94: Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F. (1994). Data submission to UniProtKB on 1994-09.

Rabinowitz08: Rabinowitz JD, Hsiao JJ, Gryncel KR, Kantrowitz ER, Feng XJ, Li G, Rabitz H (2008). "Dissecting enzyme regulation by multiple allosteric effectors: nucleotide regulation of aspartate transcarbamoylase." Biochemistry 47(21);5881-8. PMID: 18454556

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Rosenbusch71: Rosenbusch JP, Weber K (1971). "Subunit structure of aspartate transcarbamylase from Escherichia coli." J Biol Chem 246(6);1644-57. PMID: 4926546

Schachman88: Schachman HK (1988). "Can a simple model account for the allosteric transition of aspartate transcarbamoylase?." J Biol Chem 263(35);18583-6. PMID: 3058687

Silver83: Silver RS, Daigneault JP, Teague PD, Kantrowitz ER (1983). "Analysis of two purified mutants of Escherichia coli aspartate transcarbamylase with single amino acid substitutions." J Mol Biol 1983;168(4);729-45. PMID: 6350607

Stieglitz04: Stieglitz K, Stec B, Baker DP, Kantrowitz ER (2004). "Monitoring the transition from the T to the R state in E.coli aspartate transcarbamoylase by X-ray crystallography: crystal structures of the E50A mutant enzyme in four distinct allosteric states." J Mol Biol 341(3);853-68. PMID: 15288791

Stieglitz05: Stieglitz KA, Dusinberre KJ, Cardia JP, Tsuruta H, Kantrowitz ER (2005). "Structure of the E.coli aspartate transcarbamoylase trapped in the middle of the catalytic cycle." J Mol Biol 352(2);478-86. PMID: 16120448

Stieglitz05a: Stieglitz KA, Pastra-Landis SC, Xia J, Tsuruta H, Kantrowitz ER (2005). "A single amino acid substitution in the active site of Escherichia coli aspartate transcarbamoylase prevents the allosteric transition." J Mol Biol 349(2);413-23. PMID: 15890205

Stieglitz09: Stieglitz KA, Xia J, Kantrowitz ER (2009). "The first high pH structure of Escherichia coli aspartate transcarbamoylase." Proteins 74(2);318-27. PMID: 18618694

Tolonen11: Tolonen E, Bueno B, Kulshreshta S, Cieplak P, Argaez M, Velazquez L, Stec B (2011). "Allosteric transition and binding of small molecule effectors causes curvature change in central β-sheets of selected enzymes." J Mol Model 17(4);899-911. PMID: 20602244

Tsuruta94: Tsuruta H, Vachette P, Sano T, Moody MF, Amemiya Y, Wakabayashi K, Kihara H (1994). "Kinetics of the quaternary structure change of aspartate transcarbamylase triggered by succinate, a competitive inhibitor." Biochemistry 1994;33(33);10007-12. PMID: 8060968

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

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt12a: UniProt Consortium (2012). "UniProt version 2012-02 released on 2012-02-29 00:00:00." Database.

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

Van91a: Van der Graaf M, Kroon GJ, Hemminga MA (1991). "Conformation and mobility of the RNA-binding N-terminal part of the intact coat protein of cowpea chlorotic mottle virus. A two-dimensional proton nuclear magnetic resonance study." J Mol Biol 1991;220(3);701-9. PMID: 1908015

Wang05b: Wang J, Stieglitz KA, Cardia JP, Kantrowitz ER (2005). "Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase." Proc Natl Acad Sci U S A 102(25);8881-6. PMID: 15951418

Wang07e: Wang J, Eldo J, Kantrowitz ER (2007). "Structural model of the R state of Escherichia coli aspartate transcarbamoylase with substrates bound." J Mol Biol 371(5);1261-73. PMID: 17603076

Wang08: Wang Q, Xia J, Guallar V, Krilov G, Kantrowitz ER (2008). "Mechanism of thermal decomposition of carbamoyl phosphate and its stabilization by aspartate and ornithine transcarbamoylases." Proc Natl Acad Sci U S A 105(44);16918-23. PMID: 18971327

Weber68: Weber K (1968). "New structural model of E. coli aspartate transcarbamylase and the amino-acid sequence of the regulatory polypeptide chain." Nature 218(5147);1116-9. PMID: 4872216

Weitzman66: Weitzman PD, Wilson IB (1966). "Studies on aspartate transcarbamylase and its allosteric interaction." J Biol Chem 241(23);5481-8. PMID: 5333198

West04: West JM, Tsuruta H, Kantrowitz ER (2004). "A fluorescent probe-labeled Escherichia coli aspartate transcarbamoylase that monitors the allosteric conformational state." J Biol Chem 279(2);945-51. PMID: 14581486

Wild89: Wild JR, Loughrey-Chen SJ, Corder TS (1989). "In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamoylase." Proc Natl Acad Sci U S A 86(1);46-50. PMID: 2643106

Zhang91: Zhang Y, Kantrowitz ER (1991). "The synergistic inhibition of Escherichia coli aspartate carbamoyltransferase by UTP in the presence of CTP is due to the binding of UTP to the low affinity CTP sites." J Biol Chem 1991;266(33);22154-8. PMID: 1939236


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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Thu Dec 18, 2014, BIOCYC13A.