Transaminase of gamma-proteobacteriumTransaminase of gamma-proteobacterium

Structural highlights

7p3t is a 6 chain structure with sequence from Luminiphilus syltensis NOR5-1B. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.6Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

B8KQT8_9GAMM

Publication Abstract from PubMed

Despite the plethora of information on (S)-selective amine transaminases, the (R)-selective ones are still not well-studied; only a few structures are known to date, and their substrate scope is limited, apart from a few stellar works in the field. Herein, the structure of Luminiphilus syltensis (R)-selective amine transaminase is elucidated to facilitate engineering towards variants active on bulkier substrates. The V37A variant exhibited increased activity towards 1-phenylpropylamine and to activity against 1-butylamine. In contrast, the S248 and T249 positions, located on the beta-turn in the P-pocket, seem crucial for maintaining the activity of the enzyme.

Rational engineering of Luminiphilus syltensis (R)-selective amine transaminase for the acceptance of bulky substrates.,Konia E, Chatzicharalampous K, Drakonaki A, Muenke C, Ermler U, Tsiotis G, Pavlidis IV Chem Commun (Camb). 2021 Dec 3;57(96):12948-12951. doi: 10.1039/d1cc04664k. PMID:34806715[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Konia E, Chatzicharalampous K, Drakonaki A, Muenke C, Ermler U, Tsiotis G, Pavlidis IV. Rational engineering of Luminiphilus syltensis (R)-selective amine transaminase for the acceptance of bulky substrates. Chem Commun (Camb). 2021 Dec 3;57(96):12948-12951. PMID:34806715 doi:10.1039/d1cc04664k

7p3t, resolution 1.60Å

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