2.7.2.2: carbamate kinase

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For detailed information about carbamate kinase, go to the full flat file.

Word Map on EC 2.7.2.2

2.7.2.2

ornithine

deiminase

dihydrolase

citrulline

transcarbamoylase

carbamyltransferase

arcabc

n-acetyl-l-glutamate

drug development

degradation

Reaction

Synonyms

ACK, anabolic carbamyl kinase, ArcC, carbamate kinase, carbamoyl phosphokinase, carbamyl phosphokinase, catabolic carbamyl kinase, Cbk, CCK, CK, CK-like CPS, CKase, GlcK, kinase, carbamate (phosphorylating), putrescine synthase

ECTree

2 Transferases

2.7 Transferring phosphorus-containing groups

2.7.2 Phosphotransferases with a carboxy group as acceptor

2.7.2.2 carbamate kinase

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Results	in table
1107	AA Sequence
6	Application
1	CAS Registry Number
14	Cloned(Commentary)
12	Cofactor
8	Crystallization (Commentary)
8	General Information
12	General Stability
33	Inhibitors
3	kcat/KM [mM/s]
14	Ki Value [mM]
33	KM Value [mM]
2	Localization
42	Metals/Ions
13	Molecular Weight [Da]
32	Natural Substrates/ Products (Substrates)
75	Organism
7	Pathway
36	PDB ID
7	pH Optimum
4	pH Range
1	pI Value
3	Protein Variants
15	Purification (Commentary)
16	Reaction
4	Reaction Type
60	Reference
3	Source Tissue
16	Specific Activity [micromol/min/mg]
5	Storage Stability
101	Substrates and Products (Substrate)
24	Subunits
25	Synonyms
1	Systematic Name
9	Temperature Optimum [°C]
9	Temperature Stability [°C]
3	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.7.2.2 - carbamate kinase

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3 entries

purified detagged recombinant enzyme in complex with nonhydrolyzable ATP analogue, adenosine 5'-adenylyl-beta,gamma-imidodiphosphate (AMP-PNP), and with citric acid, hanging drop vapor diffusion method, mixing of 30 mg/ml protein in 50 mM Tris-HCl, pH 8.0, 0.1 M NaCl, 5 mM MgCl2, and 1 mM DTT, with an equal volume of mother liquor containing 0.4 M ammonium citrate dibasic, pH 5.0, and 21% w/v PEG 3350, soaking of crystals in 50 mM AMP-PNP, X-ray diffraction structure determination and analysis at 2.1-2.6 A resolution

Giardia intestinalis

O97438

739466

the three-dimensional structure of carbamate kinase from the human parasite Giardia lamblia is determined at 3 A resolution. The crystals belong to the monoclinic space group P21, with unit-cell parameters a = 69.77, b = 85.41, c = 102.1 A, beta = 106.8°

crystals of the pyrococcal enzyme grown in the absence or presence of MgATP (Fig. 7) diffracted with a conventional X-ray source to at least 2.6 and 2.0 Å resolution, respectively

Pyrococcus furiosus

P95474

642230