PMID- 31000168
OWN - NLM
STAT- MEDLINE
DCOM- 20190909
LR  - 20190909
IS  - 1879-0909 (Electronic)
IS  - 0141-0229 (Linking)
VI  - 126
DP  - 2019 Jul
TI  - Structure and catalytic mechanistic insight into Enterobacter aerogenes 
      acetolactate decarboxylase.
PG  - 9-17
LID - S0141-0229(18)30635-5 [pii]
LID - 10.1016/j.enzmictec.2019.03.005 [doi]
AB  - alpha-Acetolactate decarboxylase (ALDC) catalyses alpha-acetolactate into acetoin 
      (3-hydroxy-2-butanone, AC) and is considered to be the rate-limiting enzyme in 
      the synthesis of 2,3-butanediol. In this work, the enzymatic activity of ALDC 
      from Enterobacter aerogenes ALDC (E.a.-ALDC) was fully characterized with enzyme 
      kinetics, indicating a K(m) of 14.83 +/- 0.87 mM and a k(cat) of 0.81 +/- 0.09 s(-1). 
      However, compared with the activities of ALDCs reported from other bacteria, the 
      activity of E.a.-ALDC was determined to present a relatively lower value of 
      849.08 +/- 35.21 U/mg. The enzyme showed maximum activity at pH 5.5. In addition, 
      the activity of E.a.-ALDC was promoted by Mg(2+). The crystal structure of 
      E.a.-ALDC firstly solved by X-ray crystallography at resolution of 2.4 A revealed 
      a chelated zinc ion with conserved His199, His201, His212, Glu70 and Glu259. In 
      the active center, the conservative Arg150 was particularly proven to deviate 
      from the zinc ion of the active centre, by adopting a flexible conformational 
      change, resulting in a weak interaction network of the enzyme and the substrate. 
      Further in silico docking of E.a.-ALDC with two enantiomers, (R)-acetolactate and 
      (S)-acetolactate, unaltered the interaction network of E.a.-ALDC from the apo 
      structure, which confirmed the weakened role of Arg150 in the catalytic 
      properties of E.a.-ALDC. Our results reveal a unique structure-function 
      relationship of acetolactate decarboxylase and provide a fundamental basis for 
      the enzymatic synthesis of acetoin.
CI  - Copyright (c) 2019 Elsevier Inc. All rights reserved.
FAU - Ji, Fangling
AU  - Ji F
AD  - School of Life Science and Biotechnology, Dalian University of Technology, 
      Dalian, Liaoning, 116024, PR China. Electronic address: fanglingji@dlut.edu.cn.
FAU - Feng, Yanbin
AU  - Feng Y
AD  - Marine Bioengineering Group, Dalian Institute of Chemical Physics, Chinese 
      Academy of Sciences, Dalian, Liaoning, 116023, PR China.
FAU - Li, Mingyang
AU  - Li M
AD  - School of Life Science and Biotechnology, Dalian University of Technology, 
      Dalian, Liaoning, 116024, PR China.
FAU - Long, Feida
AU  - Long F
AD  - School of Life Science and Biotechnology, Dalian University of Technology, 
      Dalian, Liaoning, 116024, PR China.
FAU - Yang, Yongliang
AU  - Yang Y
AD  - School of Life Science and Biotechnology, Dalian University of Technology, 
      Dalian, Liaoning, 116024, PR China.
FAU - Wang, Tianqi
AU  - Wang T
AD  - School of Life Science and Biotechnology, Dalian University of Technology, 
      Dalian, Liaoning, 116024, PR China.
FAU - Wang, Jingyun
AU  - Wang J
AD  - School of Life Science and Biotechnology, Dalian University of Technology, 
      Dalian, Liaoning, 116024, PR China.
FAU - Bao, Yongming
AU  - Bao Y
AD  - School of Life Science and Biotechnology, Dalian University of Technology, 
      Dalian, Liaoning, 116024, PR China; School of Food and Environment Science and 
      Engineering, Dalian University of Technology, Panjin, Liaoning, 12422, PR China.
FAU - Xue, Song
AU  - Xue S
AD  - Marine Bioengineering Group, Dalian Institute of Chemical Physics, Chinese 
      Academy of Sciences, Dalian, Liaoning, 116023, PR China. Electronic address: 
      xuesong@dicp.ac.cn.
LA  - eng
PT  - Journal Article
DEP - 20190305
PL  - United States
TA  - Enzyme Microb Technol
JT  - Enzyme and microbial technology
JID - 8003761
RN  - BG4D34CO2H (Acetoin)
RN  - EC 4.1.1.- (Carboxy-Lyases)
RN  - EC 4.1.1.5 (acetolactate decarboxylase)
SB  - IM
MH  - Acetoin/*metabolism
MH  - Carboxy-Lyases/*chemistry/genetics/*metabolism
MH  - Catalysis
MH  - Cloning, Molecular
MH  - Crystallography, X-Ray
MH  - Enterobacter aerogenes/*enzymology
MH  - Models, Molecular
MH  - Protein Conformation
MH  - Structure-Activity Relationship
MH  - Substrate Specificity
OTO - NOTNLM
OT  - Enterobacter aerogenes
OT  - X-ray crystal structure
OT  - alpha-Acetolactate decarboxylase
EDAT- 2019/04/20 06:00
MHDA- 2019/09/10 06:00
CRDT- 2019/04/20 06:00
PHST- 2018/10/28 00:00 [received]
PHST- 2019/02/20 00:00 [revised]
PHST- 2019/03/04 00:00 [accepted]
PHST- 2019/04/20 06:00 [entrez]
PHST- 2019/04/20 06:00 [pubmed]
PHST- 2019/09/10 06:00 [medline]
AID - S0141-0229(18)30635-5 [pii]
AID - 10.1016/j.enzmictec.2019.03.005 [doi]
PST - ppublish
SO  - Enzyme Microb Technol. 2019 Jul;126:9-17. doi: 10.1016/j.enzmictec.2019.03.005. 
      Epub 2019 Mar 5.