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RefGenome Electronic Jamboree 2009-02 CAD

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Orthoset

Ortholog set at PPOD

EcoliWiki has included the carA gene product annotations. The CarA gene product is a subunit of the E. coli carbamoyl phosphate synthetase, but was not included in the ortholog set.

Participants

Name Group Organism(s)/Genome(s) Notes

Ruth Lovering

BHF-UCL

Human

very few papers describe human protein, have annotated hamster protein and used this for ISS

Susan Tweedie

flyBase

D. melanogaster

Varsha Khodiyar

BHF-UCL

Human

Harold Drabkin

MGI

Mouse

Doing ISO to golden hamster protein.

Brenley McIntosh

ecoliwiki

E. coli

P00968 (carB) Carbamoyl-phosphate synthase large chain

Stan Laulederkind

RGD

Rat

Debby Siegele

ecoliwiki

E. coli

P00968 (carB) Carbamoyl-phosphate synthase large chain

Rachael Huntley

GOA

Human

CAD (P27708)

Lakshmi Pillai

AgBase

G. gallus

No ortholog

Kimberly Van Auken

WormBase

C. elegans

pyr-1 (WBGene00004259)

Seval Ozkan

AgBase

other

Petra Fey

dictyBase

D. discoideum

Noticed now that dicty enzyme is rather CAD than CPS

CAD

<ejamb>573c5f77b3a094817c4e1c4a6f9b2c99.274990.C499c10bd9e5f0

CAD</ejamb>

[back to top]


Group Organism Gene Qualifier GO ID GO term name Reference(s) Evidence Code with/from Aspect Notes Status

FlyBase

Drosophila

r

GO:0004088

carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity

PMID:4218218[1]

IMP: Inferred from Mutant Phenotype

F

complete

FlyBase

Drosophila

r

GO:0004070

aspartate carbamoyltransferase activity

PMID:4218218[1]

IMP: Inferred from Mutant Phenotype

F

complete

FlyBase

Drosophila

r

GO:0006207

'de novo' pyrimidine base biosynthetic process

PMID:4218218[1]

IMP: Inferred from Mutant Phenotype

P

complete

GOA

Human

CAD

GO:0019899

enzyme binding

PMID:15326225[2]

IPI

Q99638

F

complete

BHF-UCL

Human

CAD

GO:0005829

cytosol

PMID:15890648[3]

IDA

C

complete

BHF-UCL

Human

CAD

GO:0005634

nucleus

PMID:15890648[3]

IDA

C

complete

BHF-UCL

Human

CAD

GO:0016363

nuclear matrix

PMID:9525610[4]

IDA

C

complete

BHF-UCL

Human

CAD

GO:0018107

peptidyl-threonine phosphorylation

PMID:11986331[5]

ISS: Inferred from Sequence or Structural Similarity

P08955

P

ISS from hamster protein

complete

BHF-UCL

Human

CAD

GO:0046777

protein amino acid autophosphorylation

PMID:11986331[5]

ISS: Inferred from Sequence or Structural Similarity

P08955

P

ISS from hamster protein

complete

BHF-UCL

Human

CAD

GO:0006207

'de novo' pyrimidine base biosynthetic process

PMID:19472[6]

ISS: Inferred from Sequence or Structural Similarity

P08955

P

ISS from hamster protein

complete

BHF-UCL

Human

CAD

GO:0004070

aspartate carbamoyltransferase activity

PMID:19472[6]

ISS: Inferred from Sequence or Structural Similarity

P08955

F

ISS from hamster protein

complete

BHF-UCL

Human

CAD

GO:0005524

ATP binding

PMID:11986331[5]

ISS: Inferred from Sequence or Structural Similarity

P08955

F

ISS from hamster protein

complete

BHF-UCL

Human

CAD

GO:0016597

amino acid binding

PMID:19472[6]

ISS: Inferred from Sequence or Structural Similarity

P08955

F

ISS from hamster protein

complete

BHF-UCL

Human

CAD

GO:0004088

carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity

PMID:19472[6]

ISS: Inferred from Sequence or Structural Similarity

P08955

F

ISS from hamster protein

complete

BHF-UCL

Human

CAD

GO:0004151

dihydroorotase activity

PMID:19472[6]

ISS: Inferred from Sequence or Structural Similarity

P08955

F

ISS from hamster protein

complete

FlyBase

Drosophila

r

GO:0004151

dihydroorotase activity

PMID:806025[7]

IMP: Inferred from Mutant Phenotype

F

complete

FlyBase

Drosophila

r

GO:0004070

aspartate carbamoyltransferase activity

PMID:806025[7]

IMP: Inferred from Mutant Phenotype

F

complete

FlyBase

Drosophila

r

GO:0004088

carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity

BIOSIS:11600041556

IDA: Inferred from Direct Assay

F

complete

FlyBase

Drosophila

r

GO:0016597

amino acid binding

BIOSIS:11600041556

IC: Inferred by Curator

GO:0004088

F

Or IDA? NTR: glutamine binding?

complete

FlyBase

Drosophila

r

GO:0005524

ATP binding

BIOSIS:11600041556

IC: Inferred by Curator

GO:0004088

F

Or IDA?

complete

FlyBase

Drosophila

r

GO:0006541

glutamine metabolic process

BIOSIS:11600041556

IC: Inferred by Curator

GO:0004088

P

Or IDA? What happens to glutamine in reaction is not measured.

complete

EcoliWiki

E. coli

CarB

GO:0005524

ATP binding

PMID:14718657[8]

IMP: Inferred from Mutant Phenotype

F

Compared carbamoyl phosphate synthetase activity for wild-type and mutants in ATP-binding domain.

complete

EcoliWiki

E. coli

CarB

Contributes to

GO:0004086

carbamoyl-phosphate synthase activity

PMID:14718657[8]

IDA: Inferred from Direct Assay

F

CarAB was assayed for glutamine-dependent carbamoyl phosphate synthetase activity in a coupled assay.

complete

EcoliWiki

E. coli

CarB

GO:0005515

protein binding

PMID:4358555[9]

IDA: Inferred from Direct Assay

F

CarA (light subunit) and CarB (heavy subunit) were reversibly separated using gel filtration.

complete

EcoliWiki

E. coli

CarB

GO:0004086

carbamoyl-phosphate synthase activity

PMID:3549732[10]

IDA: Inferred from Direct Assay

F

Purified CarB was assayed for carbamoyl phosphate synthetase activity and compared to the holoenzyme (consisting of CarA and CarB).

complete

EcoliWiki

E. coli

CarB

GO:0046872

metal ion binding

PMID:229896[11]

IDA: Inferred from Direct Assay

F

Carbamoyl phosphate synthetase activity was assayed in the absence (resulting in no activity) or presence of varying concentrations of divalent cations (Mg2+, Ca2+, Mg2+, Co2+, or Zn2+).

complete

EcoliWiki

E. coli

CarB

GO:0000166

nucleotide binding

PMID:10843852[12]

IMP: Inferred from Mutant Phenotype

F

Carbamoyl phosphate synthetase activity of wild-type and mutant proteins was monitored in the presence of varying concentrations of ornithine, IMP and UMP.

complete

EcoliWiki

E. coli

CarB

GO:0019856

pyrimidine base biosynthetic process

PMID:1737023[13]

IMP: Inferred from Mutant Phenotype

P

E. coli mutants were isolated that were auxotrophic for arginine and uracil and the mutations were shown to be located in the carB gene.

complete

EcoliWiki

E. coli

CarB

GO:0008652

amino acid biosynthetic process

PMID:1737023[13]

IMP: Inferred from Mutant Phenotype

P

E. coli mutants were isolated that were auxotrophic for arginine and uracil and the mutations were shown to be located in the carB gene.

complete

EcoliWiki

E. coli

CarB

GO:0004088

carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity

PMID:1737023[13]

IGI: Inferred from Genetic Interaction

EcoliWiki:carA

F

CarB mutants are unable to use ammonia or glutamine as the nitrogen donor for carbamoyl phosphate synthesis.

complete

MGI

Mouse

Cad

GO:0005737

cytoplasm

PMID:15890648[3]

ISS: Inferred from Sequence or Structural Similarity

UniProtKB:P08955

C

ISO mouse orthology to hamster

Based more on the immunohistochem than the fractionation.

complete

MGI

Mouse

Cad

GO:0005634

nucleus

PMID:15890648[3]

ISS: Inferred from Sequence or Structural Similarity

UniProtKB:P08955

C

ISO modification:MOD:00047; O-phospho-L-threonine|thr456

Phosphorylated form is nuclear

complete

MGI

Mouse

Cad

GO:0005524

ATP binding

PMID:11986331[5]

ISS: Inferred from Sequence or Structural Similarity

UniProtKB:P08955

F

ISO orthology to hamster

complete

MGI

Mouse

Cad

GO:0004070

aspartate carbamoyltransferase activity

PMID:19472[6]

ISS: Inferred from Sequence or Structural Similarity

UniProtKB:P08955

F

ISO to hamster

complete

MGI

Mouse

Cad

GO:0004151

dihydroorotase activity

PMID:19472[6]

ISS: Inferred from Sequence or Structural Similarity

UniProtKB:P08955

F

ISO hamster

complete

MGI

Mouse

Cad

GO:0004088

carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity

PMID:19472[6]

ISS: Inferred from Sequence or Structural Similarity

UniProtKB:P08955

F

ISO hamster

complete

MGI

Mouse

Cad

GO:0004672

protein kinase activity

PMID:11986331[5]

ISS: Inferred from Sequence or Structural Similarity

UniProtKB:P08955

F

ISO hamster target:P08955|thr1037

complete

MGI

Mouse

Cad

GO:0006207

'de novo' pyrimidine base biosynthetic process

PMID:19472[6]

ISS: Inferred from Sequence or Structural Similarity

UniProtKB:P08955

P

ISO to hamster

complete

MGI

Mouse

Cad

GO:0046777

protein amino acid autophosphorylation

PMID:11986331[5]

ISS: Inferred from Sequence or Structural Similarity

UniProtKB:P08955

P

ISO hamster target:P08955|thr1037

complete

MGI

Mouse

Cad

GO:0018107

peptidyl-threonine phosphorylation

PMID:11986331[5]

ISS: Inferred from Sequence or Structural Similarity

UniProtKB:P08955

P

ISO hamster target:P08955|thr1037

complete

RGD

Rat

Cad

GO:0004070

aspartate carbamoyltransferase activity

PMID:1148171[14]

IDA: Inferred from Direct Assay

F

complete

MGI

Mouse

Cad

GO:0004070

aspartate carbamoyltransferase activity

PMID:19472[6]

ISS: Inferred from Sequence or Structural Similarity

UniProtKB:P08955

F

ISO hamster

complete

RGD

Rat

Cad

GO:0004088

carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity

PMID:1148171[14]

IDA: Inferred from Direct Assay

F

complete

RGD

Rat

Cad

GO:0004151

dihydroorotase activity

PMID:1148171[14]

IDA: Inferred from Direct Assay

F

complete

RGD

Rat

Cad

GO:0042802

identical protein binding

PMID:26565[15]

IDA: Inferred from Direct Assay

F

complete

RGD

Rat

Cad

GO:0043234

protein complex

PMID:26565[15]

IDA: Inferred from Direct Assay

C

complete

RGD

Rat

Cad

GO:0005625

soluble fraction

PMID:12803[16]

IDA: Inferred from Direct Assay

C

complete

RGD

Rat

Cad

GO:0017144

drug metabolic process

PMID:18515330[17]

IDA: Inferred from Direct Assay

P

complete

RGD

Rat

Cad

GO:0009790

embryonic development

PMID:14160653[18]

IDA: Inferred from Direct Assay

P

complete

RGD

Rat

Cad

GO:0007565

female pregnancy

PMID:6020217[19]

IDA: Inferred from Direct Assay

P

complete

RGD

Rat

Cad

GO:0031100

organ regeneration

PMID:13671431[20]

IDA: Inferred from Direct Assay

P

complete

RGD

Rat

Cad

GO:0014075

response to amine stimulus

PMID:2864015[21]

IEP: Inferred from Expression Pattern

P

complete

RGD

Rat

Cad

GO:0031000

response to caffeine

PMID:6149265[22]

IEP: Inferred from Expression Pattern

P

complete

RGD

Rat

Cad

GO:0033574

response to testosterone stimulus

PMID:6030068[23]

IEP: Inferred from Expression Pattern

P

complete

MGI

Mouse

Cad

GO:0002134

UTP binding

PMID:11986331[5]

ISS: Inferred from Sequence or Structural Similarity

UniProtKB:P08955

F

New term: UTP binding ISO to hamster Based on assays of UTP allosteric inhibition of phosphorylated and non-phosphorylated species.

complete

MGI

Mouse

Cad

GO:0005829

cytosol

PMID:11986331[5]

ISS: Inferred from Sequence or Structural Similarity

UniProtKB:P08955

C

orthology to hamster. included for completeness. Term as used by them is more of a "fraction"

complete

FlyBase

Drosophila

r

GO:0004088

carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity

PMID:28118[24]

IDA: Inferred from Direct Assay

F

complete

FlyBase

Drosophila

r

GO:0043234

protein complex

PMID:28118[24]

IDA: Inferred from Direct Assay

C

complete

FlyBase

Drosophila

r

GO:0004151

dihydroorotase activity

PMID:28118[24]

IDA: Inferred from Direct Assay

F

complete

FlyBase

Drosophila

r

GO:0004070

aspartate carbamoyltransferase activity

PMID:28118[24]

IDA: Inferred from Direct Assay

F

complete

WormBase

C.elegans

pyr-1 (WBGene00004259)

GO:0019856

pyrimidine base biosynthetic process

PMID:16828468[25]

IMP: Inferred from Mutant Phenotype

WB:cu8

P

complete

FlyBase

Drosophila

r

GO:0006207

'de novo' pyrimidine base biosynthetic process

PMID:5004701[26]

IMP: Inferred from Mutant Phenotype

P

complete

WormBase

C.elegans

pyr-1 (WBGene00004259)

GO:0046132

pyrimidine ribonucleoside biosynthetic process

PMID:16828468[25]

IMP: Inferred from Mutant Phenotype

WB:cu8

P

complete

WormBase

C.elegans

pyr-1 (WBGene00004259)

GO:0009792

embryonic development ending in birth or egg hatching

PMID:16828468[25]

IMP: Inferred from Mutant Phenotype

WB:cu8

P

complete

WormBase

C.elegans

pyr-1 (WBGene00004259)

GO:0009792

embryonic development ending in birth or egg hatching

PMID:16828468[25]

IGI: Inferred from Genetic Interaction

WB:WBGene00004360

P

complete

WormBase

C.elegans

pyr-1 (WBGene00004259)

GO:0048562

embryonic organ morphogenesis

PMID:16828468[25]

IMP: Inferred from Mutant Phenotype

WB:cu8

P

complete

WormBase

C.elegans

pyr-1 (WBGene00004259)

GO:0048562

embryonic organ morphogenesis

PMID:16828468[25]

IGI: Inferred from Genetic Interaction

WB:WBGene00004360

P

complete

WormBase

C.elegans

pyr-1 (WBGene00004259)

GO:0035121

tail morphogenesis

PMID:16828468[25]

IMP: Inferred from Mutant Phenotype

WB:cu8

P

complete

WormBase

C.elegans

pyr-1 (WBGene00004259)

GO:0040010

positive regulation of growth rate

PMID:16828468[25]

IMP: Inferred from Mutant Phenotype

WB:cu8

P

complete

WormBase

C.elegans

pyr-1 (WBGene00004259)

GO:0018991

oviposition

PMID:16828468[25]

IMP: Inferred from Mutant Phenotype

WB:cu8

P

complete

WormBase

C.elegans

pyr-1 (WBGene00004259)

GO:0050891

multicellular organismal water homeostasis

PMID:16828468[25]

IMP: Inferred from Mutant Phenotype

WB:cu8

P

complete

WormBase

C.elegans

pyr-1 (WBGene00004259)

GO:0002119

nematode larval development

PMID:16828468[25]

IMP: Inferred from Mutant Phenotype

P

Based on an RNAi experiment not yet annotated in WB.

complete

WormBase

C.elegans

pyr-1 (WBGene00004259)

GO:0002119

nematode larval development

PMID:16828468[25]

IGI: Inferred from Genetic Interaction

WB:WBGene00004360

P

complete

WormBase

C.elegans

pyr-1 (WBGene00004259)

GO:0060323

head morphogenesis

PMID:16828468[25]

IMP: Inferred from Mutant Phenotype

P

Based on an RNAi experiment not yet curated in WB.

complete

WormBase

C.elegans

pyr-1 (WBGene00004259)

GO:0030036

actin cytoskeleton organization

PMID:16828468[25]

IMP: Inferred from Mutant Phenotype

WB:cu8

P

complete

WormBase

C.elegans

pyr-1 (WBGene00004259)

GO:0045104

intermediate filament cytoskeleton organization

PMID:16828468[25]

IMP: Inferred from Mutant Phenotype

WB:cu8

P

complete

WormBase

C.elegans

pyr-1 (WBGene00004259)

GO:0015012

heparan sulfate proteoglycan biosynthetic process

PMID:16828468[25]

IMP: Inferred from Mutant Phenotype

WB:cu8

P

complete

WormBase

C.elegans

pyr-1 (WBGene00004259)

GO:0050654

chondroitin sulfate proteoglycan metabolic process

PMID:16828468[25]

IMP: Inferred from Mutant Phenotype

WB:cu8

P

Chondroitin sulfate levels increase in pyr-1 mutant animals.

complete

DictyBase

Dicty

pyr1-3|DDB_G0276335

GO:0004088

carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity

PMID:2568162[27]

IDA: Inferred from Direct Assay

F

complete

DictyBase

Dicty

pyr1-3|DDB_G0276335

GO:0004070

aspartate carbamoyltransferase activity

PMID:2568162[27]

IDA: Inferred from Direct Assay

F

complete

DictyBase

Dicty

pyr1-3|DDB_G0276335

GO:0004151

dihydroorotase activity

PMID:2568162[27]

IDA: Inferred from Direct Assay

F

complete

DictyBase

Dicty

pyr1-3|DDB_G0276335

GO:0006541

glutamine metabolic process

PMID:2568162[27]

IDA: Inferred from Direct Assay

P

complete

EcoliWiki

E. coli

carA

GO:0005737

cytoplasm

PMID:2682645[28]

IDA: Inferred from Direct Assay

C

complete

EcoliWiki

E. coli

carA

GO:0005515

protein binding

PMID:2682645[28]

IMP: Inferred from Mutant Phenotype

F

complete

EcoliWiki

E. coli

carA

GO:0006541

glutamine metabolic process

PMID:1827118[29]

IMP: Inferred from Mutant Phenotype

P

complete

EcoliWiki

E. coli

carA

Contributes to

GO:0004088

carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity

PMID:1827118[29]

IMP: Inferred from Mutant Phenotype

F

complete

EcoliWiki

E. coli

carA

GO:0006207

'de novo' pyrimidine base biosynthetic process

PMID:5319709[30]

IMP: Inferred from Mutant Phenotype

P

complete

EcoliWiki

E. coli

carA

GO:0006526

arginine biosynthetic process

PMID:5319709[30]

IMP: Inferred from Mutant Phenotype

P

complete

Notes

[back to top]


Minutes

E. coli: CPS2 function annotation two genes, carA and carB, and it's complex, both annotated

Yes, annotate all here and choose what's used for propagation.

London: a term describing allosteric regulation would be useful. Allosteric (mechanics) are outside of GO scope, only the regulation part is important

  • Regulation discussion. What experiments needed to use regulation term?
  • Poll:

Would you annotate to both 'regulation of process x' and also to 'process x' for a key protein in the pathway which has also been found to regulate the whole pathway by its allosteric binding site

    • 67% yes, 11% NO, 22% Unsure

References

[back to top]


See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 Norby, S (1973) The biochemical genetics of rudimentary mutants of Drosophila melanogaster. I. Aspartate carbamoyltransferase levels in complementing and non-complementing strains. Hereditas 73 11-6 PubMed GONUTS page
  2. Lindsey-Boltz, LA et al. (2004) The human Rad9 checkpoint protein stimulates the carbamoyl phosphate synthetase activity of the multifunctional protein CAD. Nucleic Acids Res. 32 4524-30 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 Sigoillot, FD et al. (2005) Nuclear localization and mitogen-activated protein kinase phosphorylation of the multifunctional protein CAD. J. Biol. Chem. 280 25611-20 PubMed GONUTS page
  4. Angeletti, PC & Engler, JA (1998) Adenovirus preterminal protein binds to the CAD enzyme at active sites of viral DNA replication on the nuclear matrix. J. Virol. 72 2896-904 PubMed GONUTS page
  5. 5.0 5.1 5.2 5.3 5.4 5.5 5.6 5.7 5.8 Sigoillot, FD et al. (2002) Autophosphorylation of the mammalian multifunctional protein that initiates de novo pyrimidine biosynthesis. J. Biol. Chem. 277 24809-17 PubMed GONUTS page
  6. 6.0 6.1 6.2 6.3 6.4 6.5 6.6 6.7 6.8 6.9 Coleman, PF et al. (1977) Purification from hamster cells of the multifunctional protein that initiates de novo synthesis of pyrimidine nucleotides. J. Biol. Chem. 252 6379-85 PubMed GONUTS page
  7. 7.0 7.1 Rawls, JM & Fristrom, JW (1975) A complex genetic locus that controls of the first three steps of pyrimidine biosynthesis in Drosophila. Nature 255 738-40 PubMed GONUTS page
  8. 8.0 8.1 Kothe, M & Powers-Lee, SG (2004) Nucleotide recognition in the ATP-grasp protein carbamoyl phosphate synthetase. Protein Sci. 13 466-75 PubMed GONUTS page
  9. Trotta, PP et al. (1974) Reversible dissociation of the monomer of glutamine-dependent carbamyl phosphate synthetase into catalytically active heavy and light subunits. J. Biol. Chem. 249 492-9 PubMed GONUTS page
  10. Rubino, SD et al. (1987) In vivo synthesis of carbamyl phosphate from NH3 by the large subunit of Escherichia coli carbamyl phosphate synthetase. J. Biol. Chem. 262 4382-6 PubMed GONUTS page
  11. Raushel, FM et al. (1979) Paramagnetic probes for carbamoyl-phosphate synthetase: metal ion binding studies and preparation of nitroxide spin-labeled derivatives. Biochemistry 18 5562-6 PubMed GONUTS page
  12. Fresquet, V et al. (2000) Site-directed mutagenesis of the regulatory domain of Escherichia coli carbamoyl phosphate synthetase identifies crucial residues for allosteric regulation and for transduction of the regulatory signals. J. Mol. Biol. 299 979-91 PubMed GONUTS page
  13. 13.0 13.1 13.2 Guillou, F et al. (1992) Mutational analysis of carbamyl phosphate synthetase. Substitution of Glu841 leads to loss of functional coupling between the two catalytic domains of the synthetase subunit. Biochemistry 31 1656-64 PubMed GONUTS page
  14. 14.0 14.1 14.2 Mori, M et al. (1975) Aggregation states and catalytic properties of the multienzyme complex catalyzing the initial steps of pyrimidine biosynthesis in rat liver. Biochemistry 14 2622-30 PubMed GONUTS page
  15. 15.0 15.1 Mori, M & Tatibana, M (1978) Multi-enzyme complex of glutamine-dependent carbamoyl-phosphate synthetase with aspartate carbamoyltransferase and dihydroorotase from rat ascites-hepatoma cells. Purification, molecular properties and limited proteolysis. Eur. J. Biochem. 86 381-8 PubMed GONUTS page
  16. Bond, JS (1976) Acid inactivation of short-lived rat liver enzymes. Biochim. Biophys. Acta 451 238-49 PubMed GONUTS page
  17. Schroeder, PE et al. (2008) The dihydroorotase inhibitor 5-aminoorotic acid inhibits the metabolism in the rat of the cardioprotective drug dexrazoxane and its one-ring open metabolites. Drug Metab. Dispos. 36 1780-5 PubMed GONUTS page
  18. NORDMANN, Y et al. (1964) ACTIVITY OF ASPARTATE TRANSCARBAMYLASE IN HEART AND LIVER OF THE DEVELOPING RAT. Nature 201 616-7 PubMed GONUTS page
  19. Thibodeau, PS & Thayer, SA (1967) Effect of pregnancy and hormones on the activity of aspartate transcarbamylase and the level of nucleic acids in the mammary gland of the rat. Endocrinology 80 505-9 PubMed GONUTS page
  20. CALVA, E & COHEN, PP (1959) Carbamyl phosphate-aspartate transcarbamylase activity in regenerating rat liver. Cancer Res. 19 679-83 PubMed GONUTS page
  21. Karsai, T et al. () Effect of dimethylnitrosamine upon carbamoyl phosphate and ornithine utilization in rat liver. Anticancer Res. 5 441-4 PubMed GONUTS page
  22. Miñana, MD et al. (1984) Lesch-Nyhan syndrome, caffeine model: increase of purine and pyrimidine enzymes in rat brain. J. Neurochem. 43 1556-60 PubMed GONUTS page
  23. Görlich, M & Heise, E (1967) Activity of aspartate transcarbamylase in mammary tumours induced by 7,12-dimethyl-benzanthracene in the rat. Nature 213 934-5 PubMed GONUTS page
  24. 24.0 24.1 24.2 24.3 Brothers, VM et al. (1978) Rudimentary locus of Drosophila melanogaster: partial purification of a carbamylphosphate synthase--aspartate transcarbamylase--dihydroorotase complex. Biochem. Genet. 16 321-32 PubMed GONUTS page
  25. 25.00 25.01 25.02 25.03 25.04 25.05 25.06 25.07 25.08 25.09 25.10 25.11 25.12 25.13 25.14 25.15 25.16 Franks, DM et al. (2006) C. elegans pharyngeal morphogenesis requires both de novo synthesis of pyrimidines and synthesis of heparan sulfate proteoglycans. Dev. Biol. 296 409-20 PubMed GONUTS page
  26. Norby, S (1970) A specific nutritional requirement for pyrimidines in rudimentary mutants of Drosophila melanogaster. Hereditas 66 205-14 PubMed GONUTS page
  27. 27.0 27.1 27.2 27.3 Wales, ME et al. (1989) Characterization of pyrimidine metabolism in the cellular slime mold, Dictyostelium discoideum. Can. J. Microbiol. 35 432-8 PubMed GONUTS page
  28. 28.0 28.1 Guillou, F et al. (1989) Escherichia coli carbamoyl-phosphate synthetase: domains of glutaminase and synthetase subunit interaction. Proc. Natl. Acad. Sci. U.S.A. 86 8304-8 PubMed GONUTS page
  29. 29.0 29.1 Mullins, LS et al. (1991) Alterations in the energetics of the carbamoyl phosphate synthetase reaction by site-directed modification of the essential sulfhydryl group. J. Biol. Chem. 266 8236-40 PubMed GONUTS page
  30. 30.0 30.1 Piérard, A & Wiame, JM (1964) Regulation and mutation affecting a glutamine dependent formation of carbamyl phosphate in Escherichia coli. Biochem. Biophys. Res. Commun. 15 76-81 PubMed GONUTS page