5.4.3.11: phenylalanine aminomutase (D-beta-phenylalanine forming)

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For detailed information about phenylalanine aminomutase (D-beta-phenylalanine forming), go to the full flat file.

Reaction

Synonyms

admH, EncP, HitA, methylidene imidazolone-dependent phenylalanine aminomutase, MIO-dependent phenylalanine ammonia lyase, PAM, PaPAM, phenylalanine 2,3-aminomutase, phenylalanine aminomutase, phenylalanine-2,3-aminomutase

ECTree

     5 Isomerases

         5.4 Intramolecular transferases

             5.4.3 Transferring amino groups

                5.4.3.11 phenylalanine aminomutase (D-beta-phenylalanine forming)

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Results	in table
2	Activating Compound
24	AA Sequence
4	Application
7	Cloned(Commentary)
3	Cofactor
1	Crystallization (Commentary)
9	General Information
1	General Stability
24	kcat/KM [mM/s]
25	KM Value [mM]
1	Metals/Ions
5	Natural Substrates/ Products (Substrates)
12	Organism
4	pH Optimum
1	pH Stability
5	Protein Variants
4	Purification (Commentary)
3	Reaction
1	Reaction Type
11	Reference
53	Substrates and Products (Substrate)
2	Subunits
28	Synonyms
1	Systematic Name
8	Temperature Optimum [°C]
4	Temperature Stability [°C]
24	Turnover Number [1/s]

Crystallization

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Crystallization on EC 5.4.3.11 - phenylalanine aminomutase (D-beta-phenylalanine forming)

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

to 1.7 A resolution with cinnamate included in the crystallization buffer. The monomer consists of mostly alphahelices that run parallel to one another and form a four-helix bundle at the center. The catalytically relevant species is a dimer of dimers, in which the two monomers in the asymmetric unit are related by a crystallographic twofold axis to the other two monomers that comprise the catalytically functional tetramer, and each subunit contains an active site. During the reaction, the phenylpropanoid carbon backbone remains mostly stationary above the amino group that is attached to the cofactor moiety

Pantoea agglomerans

Q84FL5

721286