PMID- 31731965
OWN - NLM
STAT- MEDLINE
DCOM- 20200409
LR  - 20200409
IS  - 1879-0909 (Electronic)
IS  - 0141-0229 (Linking)
VI  - 132
DP  - 2020 Jan
TI  - Broadening the repertoire of microbial aldo-keto reductases: cloning and 
      characterization of AKR3B4 from Rhodotorula mucilaginosa LSL strain.
PG  - 109415
LID - S0141-0229(19)30153-X [pii]
LID - 10.1016/j.enzmictec.2019.109415 [doi]
AB  - Aldo-keto reductases (AKRs) are nicotinamide-dependent enzymes that catalyze the 
      transformation of aldehydes and ketones into alcohols. They are spread across all 
      phyla, and those from microbial origin have proved to be highly robust and 
      versatile biocatalysts. In this work, we have discovered and characterized a 
      microbial AKR from the yeast Rhodotorula mucilaginosa by combining genome-mining 
      and expression assays. The new enzyme, named AKR3B4, was expressed by a simple 
      protocol in very good amounts. It displays a selective substrate profile 
      exclusively transforming aldehydes into alcohols. Also, AKR3B4 shows very good 
      stability at medium temperatures, in a broad range of pH values and in the 
      presence of green organic solvents. Conversion assays demonstrate it is an 
      excellent biocatalyst to be used in the synthesis of aromatic alcohols, and also 
      to produce furan-3-ylmethanol and the valuable sweetener xylitol. These results 
      show that AKR3B4 displays attractive features so as to be used in chemoenzymatic 
      processes.
CI  - Copyright (c) 2019 Elsevier Inc. All rights reserved.
FAU - Anello, Abi L
AU  - Anello AL
AD  - IMIBIO-SL CONICET, Facultad de Quimica Bioquimica y Farmacia, Universidad 
      Nacional de San Luis, Ejercito de los Andes 950, D5700HHW, San Luis, Argentina; 
      INTEQUI CONICET, Facultad de Quimica Bioquimica y Farmacia, Universidad Nacional 
      de San Luis, Almirante Brown 1455, D5700HHW, San Luis, Argentina.
FAU - Aguilera, Leonardo
AU  - Aguilera L
AD  - INTEQUI CONICET, Facultad de Quimica Bioquimica y Farmacia, Universidad Nacional 
      de San Luis, Almirante Brown 1455, D5700HHW, San Luis, Argentina.
FAU - Kurina-Sanz, Marcela
AU  - Kurina-Sanz M
AD  - INTEQUI CONICET, Facultad de Quimica Bioquimica y Farmacia, Universidad Nacional 
      de San Luis, Almirante Brown 1455, D5700HHW, San Luis, Argentina.
FAU - Juri Ayub, Maximiliano
AU  - Juri Ayub M
AD  - IMIBIO-SL CONICET, Facultad de Quimica Bioquimica y Farmacia, Universidad 
      Nacional de San Luis, Ejercito de los Andes 950, D5700HHW, San Luis, Argentina.
FAU - Mascotti, Maria Laura
AU  - Mascotti ML
AD  - IMIBIO-SL CONICET, Facultad de Quimica Bioquimica y Farmacia, Universidad 
      Nacional de San Luis, Ejercito de los Andes 950, D5700HHW, San Luis, Argentina. 
      Electronic address: mlmascotti@unsl.edu.ar.
LA  - eng
PT  - Journal Article
DEP - 20190821
PL  - United States
TA  - Enzyme Microb Technol
JT  - Enzyme and microbial technology
JID - 8003761
RN  - 0 (Alcohols)
RN  - 0 (Aldehydes)
RN  - 0 (Enzymes)
RN  - 0 (Fungal Proteins)
RN  - EC 1.1.- (Alcohol Oxidoreductases)
RN  - EC 1.1.1.- (Aldo-Keto Reductases)
RN  - EC 1.1.1.21 (Aldehyde Reductase)
SB  - IM
MH  - Alcohol Oxidoreductases/metabolism
MH  - Alcohols/metabolism
MH  - Aldehyde Reductase/metabolism
MH  - Aldehydes/metabolism
MH  - Aldo-Keto Reductases/*genetics/*metabolism
MH  - Cloning, Molecular
MH  - Enzymes
MH  - Fungal Proteins/genetics/metabolism
MH  - Rhodotorula/*enzymology/*genetics
MH  - Substrate Specificity
OTO - NOTNLM
OT  - Aldo-keto reductases
OT  - Aromatic aldehydes
OT  - Carbonyl
OT  - Rhodotorula
OT  - Yeast
EDAT- 2019/11/17 06:00
MHDA- 2020/04/10 06:00
CRDT- 2019/11/17 06:00
PHST- 2019/06/21 00:00 [received]
PHST- 2019/08/13 00:00 [revised]
PHST- 2019/08/20 00:00 [accepted]
PHST- 2019/11/17 06:00 [entrez]
PHST- 2019/11/17 06:00 [pubmed]
PHST- 2020/04/10 06:00 [medline]
AID - S0141-0229(19)30153-X [pii]
AID - 10.1016/j.enzmictec.2019.109415 [doi]
PST - ppublish
SO  - Enzyme Microb Technol. 2020 Jan;132:109415. doi: 10.1016/j.enzmictec.2019.109415. 
      Epub 2019 Aug 21.