4BT4
acetolactate decarboxylase with a bound (2S,3S)-2,3-Dihydroxy-2- methylbutanoic acid
Summary for 4BT4
| Entry DOI | 10.2210/pdb4bt4/pdb |
| Related | 4BT2 4BT3 4BT5 4BT6 4BT7 |
| Descriptor | ALPHA-ACETOLACTATE DECARBOXYLASE, ZINC ION, (2S,3S)-2,3-dihydroxy-2-methylbutanoic acid, ... (4 entities in total) |
| Functional Keywords | lyase, acetoin biosynthesis, stereoselective decarboxylation, bifunctional enzyme |
| Biological source | BREVIBACILLUS BREVIS |
| Total number of polymer chains | 1 |
| Total formula weight | 29030.16 |
| Authors | A Marlow, V.,Rea, D.,Najmudin, S.,Wills, M.,Fulop, V. (deposition date: 2013-06-12, release date: 2013-09-11, Last modification date: 2023-12-20) |
| Primary citation | Marlow, V.A.,Rea, D.,Najmudin, S.,Wills, M.,Fulop, V. Structure and Mechanism of Acetolactate Decarboxylase. Acs Chem.Biol., 8:2339-, 2013 Cited by PubMed Abstract: Acetolactate decarboxylase catalyzes the conversion of both enantiomers of acetolactate to the (R)-enantiomer of acetoin, via a mechanism that has been shown to involve a prior rearrangement of the non-natural (R)-enantiomer substrate to the natural (S)-enantiomer. In this paper, a series of crystal structures of ALDC complex with designed transition state mimics are reported. These structures, coupled with inhibition studies and site-directed mutagenesis provide an improved understanding of the molecular processes involved in the stereoselective decarboxylation/protonation events. A mechanism for the transformation of each enantiomer of acetolactate is proposed. PubMed: 23985082DOI: 10.1021/CB400429H PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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