4CMF

The (R)-selective transaminase from Nectria haematococca with inhibitor bound

Summary for 4CMF

• Entry DOI: 10.2210/pdb4cmf/pdb
• Related: 4CMD
• Descriptor: AMINOTRANSFERASE, 3-[O-PHOSPHONOPYRIDOXYL]--AMINO-BENZOIC ACID, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (5 entities in total)
• Functional Keywords: transferase
• Biological source: NECTRIA HAEMATOCOCCA MPVI
• Total number of polymer chains: 1
• Total formula weight: 36850.11

Authors

Sayer, C.,Isupov, M.,Martinez-Torres, R.J.,Richter, N.,Hailes, H.C.,Ward, J.,Littlechild, J. (deposition date: 2014-01-16, release date: 2014-03-26, Last modification date: 2023-12-20)

Primary citation

Sayer, C.,Martinez-Torres, R.J.,Richter, N.,Isupov, M.N.,Hailes, H.C.,Littlechild, J.A.,Ward, J.M.
The Substrate Specificity, Enantioselectivity and Structure of the (R)-Selective Amine:Pyruvate Transaminase from Nectria Haematococca.
FEBS J., 281:2240-, 2014

PubMed Abstract: During the last decade the use of transaminases for the production of pharmaceutical and fine chemical intermediates has attracted a great deal of attention. Transaminases are versatile biocatalysts for the efficient production of amine intermediates and many have (S)-enantiospecificity. Transaminases with (R)-specificity are needed to expand the applications of these enzymes in biocatalysis. In this work we have identified a fungal putative (R)-specific transaminase from the Eurotiomycetes Nectria haematococca, cloned a synthetic version of this gene, demonstrated (R)-selective deamination of several substrates including (R)-α-methylbenzylamine, as well as production of (R)-amines, and determined its crystal structure. The crystal structures of the holoenzyme and the complex with an inhibitor gabaculine offer the first detailed insight into the structural basis for substrate specificity and enantioselectivity of the industrially important class of (R)-selective amine : pyruvate transaminases.

PubMed: 24618038
DOI: 10.1111/FEBS.12778

Experimental method

X-RAY DIFFRACTION (1.5 Å)