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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
3.5.4.30
733177
Bacillus halodurans strain C125 encodes and synthesizes enzymes from both known pathways to form dump directly from cytosine deoxyribonucleotides
Appl. Environ. Microbiol.
81
3395-3404
2015
Halalkalibacterium halodurans
25746996
3.5.4.30
733177
Bacillus halodurans strain C125 encodes and synthesizes enzymes from both known pathways to form dump directly from cytosine deoxyribonucleotides
Appl. Environ. Microbiol.
81
3395-3404
2015
Halalkalibacterium halodurans C-125
25746996
3.5.4.30
711005
Concerted bifunctionality of the dCTP deaminase-dUTPase from Methanocaldococcus jannaschii: a structural and pre-steady state kinetic analysis
Arch. Biochem. Biophys.
490
42-49
2009
Methanocaldococcus jannaschii
19683509
3.5.4.30
648212
Structural basis for recognition and catalysis by the bifunctional dCTP deaminase and dUTPase from Methanococcus jannaschii
J. Mol. Biol.
331
885-896
2003
Methanocaldococcus jannaschii
12909016
3.5.4.30
727842
Structure of the bifunctional dCTP deaminase-dUTPase from Methanocaldococcus jannaschii and its relation to other homotrimeric dUTPases
J. Biol. Chem.
278
27916-27922
2003
Methanocaldococcus jannaschii
12756253
3.5.4.30
727842
Structure of the bifunctional dCTP deaminase-dUTPase from Methanocaldococcus jannaschii and its relation to other homotrimeric dUTPases
J. Biol. Chem.
278
27916-27922
2003
Methanocaldococcus jannaschii DSM 2661
12756253
3.5.4.30
669375
Structures of dCTP deaminase from Escherichia coli with bound substrate and product: reaction mechanism and determinants of mono- and bifunctionality for a family of enzymes
J. Biol. Chem.
280
3051-3059
2005
Escherichia coli
15539408
3.5.4.30
648211
The Methanococcus jannaschii dCTP deaminase is a bifunctional deaminase and diphosphatase
J. Biol. Chem.
278
11100-11106
2003
Methanocaldococcus jannaschii
12538648
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