4.2.3.61: 5-epiaristolochene synthase

This is an abbreviated version!
For detailed information about 5-epiaristolochene synthase, go to the full flat file.

Reaction

Synonyms

5EAT, EAS, EAS12, EAS3, EAS34, EAS37, EAS4, g110, TEAS

ECTree

4 Lyases

4.2 Carbon-oxygen lyases

4.2.3 Acting on phosphates

4.2.3.61 5-epiaristolochene synthase

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Results	in table
13	AA Sequence
3	Application
6	Cloned(Commentary)
1	Crystallization (Commentary)
1	Expression
3	kcat/KM [mM/s]
8	KM Value [mM]
1	Metals/Ions
12	Organism
2	Pathway
19	PDB ID
4	Protein Variants
1	Purification (Commentary)
1	Reaction
11	Reference
2	Source Tissue
9	Substrates and Products (Substrate)
9	Synonyms
1	Systematic Name
2	Temperature Range [°C]
2	Temperature Stability [°C]
5	Turnover Number [1/s]

Crystallization

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of the Enzyme Summary Page.

Crystallization on EC 4.2.3.61 - 5-epiaristolochene synthase

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to 2.2-2.8 A resolution, of TEAS alone and in complexes with two different substrate analogs. TEAS consists entirely of alpha-helices and short connecting loops and turns, and is organized into two structural domains. Two Mg2+ ions are coordinated on opposite sides of the entrance to the active site pocket, and constitute a diphosphate binding site. Asp301 coordinates a Mg2+ in the native TEAS structure, and the side chain carboxyl of Glu379 provides a longer range interaction. Asp305 provides an additional coordination bond in the enzyme with substrate analogs bound. Asp301 and Asp305 are part of a -DDXXD- sequence. Asp301 directly contacts Mg2+, whereas Asp302 demonstrates no direct metal coordination. The side chains of Asp444, Thr448, Glu452, and one water molecule the second coordinate Mg2+. In the native TEAS structure, the A-C and J-K loops and the residues NH2-terminal of residue 36 are disordered

Nicotiana tabacum

Q40577

713507