2.6.1.79: glutamate-prephenate aminotransferase

This is an abbreviated version!
For detailed information about glutamate-prephenate aminotransferase, go to the full flat file.

Reaction

Synonyms

1beta AAT, 1beta AAT prephenate aminotransferase, 1beta aspartate aminotransferase, aatA, aspartate aminotransferase A, aspartate/prephenate aminotransferase, AspB2, AT-C, Ath-PAT, AtPAT, bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase, class Ibeta AAT, IlvE, More, Pat, prephenate aminotransferase, prephenate: glutamate aminotransferase, Rme-AAT, Rme-AAT/PAT

ECTree

2 Transferases

2.6 Transferring nitrogenous groups

2.6.1 Transaminases

2.6.1.79 glutamate-prephenate aminotransferase

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Results	in table
22	AA Sequence
1	CAS Registry Number
3	Cloned(Commentary)
13	Cofactor
3	Crystallization (Commentary)
7	General Information
3	General Stability
2	IC50 Value
3	Inhibitors
11	KM Value [mM]
2	Localization
2	Molecular Weight [Da]
13	Natural Substrates/ Products (Substrates)
19	Organism
9	Pathway
14	PDB ID
5	pH Optimum
1	pH Range
1	pI Value
10	Protein Variants
5	Purification (Commentary)
2	Reaction
19	Reference
17	Source Tissue
14	Specific Activity [micromol/min/mg]
2	Storage Stability
66	Substrates and Products (Substrate)
2	Subunits
40	Synonyms
1	Systematic Name
5	Temperature Optimum [°C]
2	Temperature Range [°C]
10	Temperature Stability [°C]
5	Turnover Number [1/s]

Subunits

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Subunits on EC 2.6.1.79 - glutamate-prephenate aminotransferase

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x * 43000, SDS-PAGE

homodimer

AtPAT crystallizes as a homodimer. Each monomer of AtPAT consists of 15 alpha-helices and 9 beta-strands divided between two structural domains. The N-terminal domain (Lys115-Leu353) contains two sets of three a-helices surrounding six parallel and one anti-parallel beta-strand. Two additional alpha-helices in the PLP-binding pocket, as well as the a-helix connecting the N- and C-terminal domains, complete the N-terminal domain. The smaller C-terminal domain contains part of the N-terminal region (Ser71-Pro114) and residues Gly354 through Leu469, totaling five alpha-helices and two beta-strands. The N-terminal flexible loop (Ser71-Ser82) and features of the N-terminal domain form the dimer interface

759965