2.7.7.53: ATP adenylyltransferase

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For detailed information about ATP adenylyltransferase, go to the full flat file.

Reaction

Synonyms

5',5'''-P1,P4-tetraphosphate phosphorylase, adenine triphosphate adenylyltransferase, adenylyltransferase, adenine triphosphate, AP-4-A phosphorylase, Ap3A/Ap4A phosphorylase, Ap4A phosphorylase, bis(5'-nucleosyl)-tetraphosphate phosphorylase (NDP-forming), diadenosine 5',5'''-P1,P4-tetraphosphate alpha,beta-phosphorylase, diadenosine 5',5'''-P1,P4-tetraphosphate alpha,beta-phosphorylase (ADP-forming), diadenosine 5',5'''-P1,P4-tetraphosphate alphabeta-phosphorylase (ADP-forming), diadenosine 5',5'''-P1,P4-tetraphosphate phosphorylase, diadenosinetetraphosphate alpha,beta-phosphorylase, diadenosinetetraphosphate alphabeta-phosphorylase, dinucleoside oligophosphate alphabeta-phosphorylase, MAV_3489, MEG_2932, Rv2613c

ECTree

     2 Transferases

         2.7 Transferring phosphorus-containing groups

             2.7.7 Nucleotidyltransferases

                2.7.7.53 ATP adenylyltransferase

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Results	in table
908	AA Sequence
1	CAS Registry Number
4	Cloned(Commentary)
1	Crystallization (Commentary)
3	General Information
4	General Stability
21	IC50 Value
62	Inhibitors
5	kcat/KM [mM/s]
3	Ki Value [mM]
32	KM Value [mM]
50	Metals/Ions
12	Molecular Weight [Da]
4	Natural Substrates/ Products (Substrates)
42	Organism
2	Pathway
10	PDB ID
17	pH Optimum
3	pH Range
15	Protein Variants
7	Purification (Commentary)
1	Reaction
1	Reaction Type
30	Reference
10	Specific Activity [micromol/min/mg]
1	Storage Stability
158	Substrates and Products (Substrate)
9	Subunits
32	Synonyms
1	Systematic Name
11	Temperature Optimum [°C]
1	Temperature Stability [°C]
6	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.7.7.53 - ATP adenylyltransferase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

crystal structure at 1.89 A resolution by using single-wavelength anomalous dispersion. Asn139, Gly146, and Ser147 are important active-site residues, Asn139 has a critical role in catalysis. The position of Gly146 might influence the phosphorylase activity. The tetrameric structure and the presence of Trp160 might be essential for the formation of the Ap4A binding site

Mycobacterium tuberculosis

P9WMK9

722980