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Search results 101 to 123 out of 123 for Cpa2

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0.019s

Type

Details

Score

Publication

2982857 | -

First Author:	Zalkin H
Year:	1985
Journal:	J Biol Chem
Title:	Identification of a trpG-related glutamine amide transfer domain in Escherichia coli GMP synthetase.
Volume:	260
Issue:	6
Pages:	3350-4

•

Protein Domain

IPR017926 | GATASE

Type:

Domain

Description:

Glutamine amidotransferase (GATase) enzymes catalyse the removal of the ammonia group from glutamine and then transfer this group to a substrate to form a new carbon-nitrogen group []. The GATase domain exists either as a separate polypeptidic subunit or as part of a larger polypeptide fused in different ways to a synthase domain. Two classes of GATase domains have been identified [, ]: class-I (also known as trpG-type or triad) and class-II (also known as purF-type or Ntn). Class-I (or type 1) GATase domains have been found in the following enzymes:The second component of anthranilate synthase (AS) []. AS catalyzes the biosynthesis of anthranilate from chorismate and glutamine. AS is generally a dimeric enzyme: the first component can synthesize anthranilate using ammonia rather than glutamine, whereas component II provides the GATase activity []. In some bacteria and in fungi the GATase component of AS is part of a multifunctional protein that also catalyzes other steps of the biosynthesis of tryptophan.The second component of 4-amino-4-deoxychorismate (ADC) synthase, a dimeric prokaryotic enzyme that functions in the pathway that catalyzes the biosynthesis of para-aminobenzoate (PABA) from chorismate and glutamine. The second component (gene pabA) provides the GATase activity [].CTP synthase. CTP synthase catalyzes the final reaction in the biosynthesis of pyrimidine, the ATP-dependent formation of CTP from UTP and glutamine. CTP synthase is a single chain enzyme that contains two distinct domains; the GATase domain is in the C-terminal section [].GMP synthase (glutamine-hydrolyzing). GMP synthase catalyzes the ATP-dependent formation of GMP from xanthosine 5'-phosphate and glutamine. GMP synthase is a single chain enzyme that contains two distinct domains; the GATase domain is in the N-terminal section [, ].Glutamine-dependent carbamoyl-phosphate synthase (GD-CPSase); an enzyme involved in both arginine and pyrimidine biosynthesis and which catalyzes the ATP-dependent formation of carbamoyl phosphate from glutamine and carbon dioxide. In bacteria GD-CPSase is composed of two subunits: the large chain (gene carB) provides the CPSase activity, while the small chain (gene carA) provides the GATase activity. In yeast the enzyme involved in arginine biosynthesis is also composed of two subunits: CPA1 (GATase), and CPA2 (CPSase). In most eukaryotes, the first three steps of pyrimidine biosynthesis are catalyzed by a large multifunctional enzyme (called URA2 in yeast, rudimentary in Drosophila, and CAD in mammals). The GATase domain is located at the N-terminal extremity of this polyprotein [].Phosphoribosylformylglycinamidine synthase, an enzyme that catalyzes the fourth step in the de novo biosynthesis of purines. In some species of bacteria and rchaea, FGAM synthase II is composed of two subunits: a small chain (gene purQ) which provides the GATase activity and a large chain (gene purL) which provides the aminator activity. In eukaryotes and Gram-negative bacteria a single polypeptide (large type of purL) contains a FGAM synthethase domain and the GATase as the C-terminal domain [].Imidazole glycerol phosphate synthase subunit hisH, an enzyme that catalyzes the fifth step in the biosynthesis of histidine.A triad of conserved Cys-His-Glu forms the active site, wherein the catalytic cysteine is essential for the amidotransferase activity [, ]. Different structures show that the active site Cys of type 1 GATase is located at the tip of a nucleophile elbow.

•

Protein

A2AEQ5

Organism:	Mus musculus/domesticus
Length:	151
Fragment?:	false

•

Protein

Q3THK7

Organism:	Mus musculus/domesticus
Length:	693
Fragment?:	false

•

Protein

P70698

Organism:	Mus musculus/domesticus
Length:	591
Fragment?:	false

•

Protein

P70303

Organism:	Mus musculus/domesticus
Length:	586
Fragment?:	false

•

Protein

B2RRH9

Organism:	Mus musculus/domesticus
Length:	693
Fragment?:	false

•

Publication

10449718 | -

First Author:	Knöchel T
Year:	1999
Journal:	Proc Natl Acad Sci U S A
Title:	The crystal structure of anthranilate synthase from Sulfolobus solfataricus: functional implications.
Volume:	96
Issue:	17
Pages:	9479-84

•

Publication

15301531 | -

First Author:	Anand R
Year:	2004
Journal:	Biochemistry
Title:	Domain organization of Salmonella typhimurium formylglycinamide ribonucleotide amidotransferase revealed by X-ray crystallography.
Volume:	43
Issue:	32
Pages:	10328-42

•

Publication

8548458 | -

First Author:	Tesmer JJ
Year:	1996
Journal:	Nat Struct Biol
Title:	The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families.
Volume:	3
Issue:	1
Pages:	74-86

•

Publication

2679363 | -

First Author:	Crawford IP
Year:	1989
Journal:	Annu Rev Microbiol
Title:	Evolution of a biosynthetic pathway: the tryptophan paradigm.
Volume:	43

Pages:	567-600

•

Publication

3298209 | -

First Author:	Weng ML
Year:	1987
Journal:	J Bacteriol
Title:	Structural role for a conserved region in the CTP synthetase glutamine amide transfer domain.
Volume:	169
Issue:	7
Pages:	3023-8

•

Publication

6086650 | -

First Author:	Nyunoya H
Year:	1984
Journal:	J Biol Chem
Title:	Sequence of the small subunit of yeast carbamyl phosphate synthetase and identification of its catalytic domain.
Volume:	259
Issue:	15
Pages:	9790-8

•

Publication

4355768 | -

First Author:	Buchanan JM
Year:	1973
Journal:	Adv Enzymol Relat Areas Mol Biol
Title:	The amidotransferases.
Volume:	39

Pages:	91-183

•

Publication

9575335 | -

First Author:	Massière F
Year:	1998
Journal:	Cell Mol Life Sci
Title:	The mechanism of glutamine-dependent amidotransferases.
Volume:	54
Issue:	3
Pages:	205-22

•

Protein

Q7TN13

Organism:	Mus musculus/domesticus
Length:	1019
Fragment?:	true

•

Protein

E9QAT6

Organism:	Mus musculus/domesticus
Length:	971
Fragment?:	false

•

Publication

8098212 | -

First Author:	Davidson JN
Year:	1993
Journal:	Bioessays
Title:	The evolutionary history of the first three enzymes in pyrimidine biosynthesis.
Volume:	15
Issue:	3
Pages:	157-64

•

Protein

Q8C196

Organism:	Mus musculus/domesticus
Length:	1500
Fragment?:	false

•

Protein

B2RQC6

Organism:	Mus musculus/domesticus
Length:	2225
Fragment?:	false

•

Protein

E9QAI5

Organism:	Mus musculus/domesticus
Length:	2162
Fragment?:	false

•

Protein

G3UWN2

Organism:	Mus musculus/domesticus
Length:	2164
Fragment?:	false

•

Publication

14705960 | -

First Author:	Rawlings ND
Year:	2004
Journal:	Biochem J
Title:	Evolutionary families of peptidase inhibitors.
Volume:	378
Issue:	Pt 3
Pages:	705-16

•

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