PMID- 27542750
OWN - NLM
STAT- MEDLINE
DCOM- 20170509
LR  - 20170509
IS  - 1879-0909 (Electronic)
IS  - 0141-0229 (Linking)
VI  - 92
DP  - 2016 Oct
TI  - A sialic acid aldolase from Peptoclostridium difficile NAP08 with 
      4-hydroxy-2-oxo-pentanoate aldolase activity.
PG  - 99-106
LID - S0141-0229(16)30132-6 [pii]
LID - 10.1016/j.enzmictec.2016.07.003 [doi]
AB  - Sialic acid aldolases (E.C.4.1.3.3) catalyze the reversible aldol cleavage of 
      N-acetyl-d-neuraminic acid (Neu5Ac) to from N-acetyl-d-mannosamine (ManNAc) and 
      pyruvate. In this study, a sialic acid aldolase (PdNAL) from Peptoclostridium 
      difficile NAP08 was expressed in Escherichia coli BL21 (DE3). This homotetrameric 
      enzyme was purified with a specific activity of 18.34U/mg for the cleavage of 
      Neu5Ac. The optimal pH and temperature for aldol addition reaction were 7.4 and 
      65 degrees C, respectively. PdNAL was quite stable at neutral and alkaline pH (6.0-10.0) 
      and maintained about 89% of the activity after incubation at pH 10.0 for 24h. 
      After incubation at 70 degrees C for 15min, almost no activity loss was observed. The 
      high thermostability simplified the purification of this enzyme. Interestingly, 
      substrate profiling showed that PdNAL not only accepted ManNAc but also short 
      chain aliphatic aldehydes such as acetaldehyde, propionaldehyde and 
      n-butyraldehyde as the substrates. This is the first example that a sialic acid 
      aldolase is active toward aliphatic aldehyde acceptors with two or more carbons. 
      The amino acid sequence analysis indicates that PdNAL belongs to the NAL 
      subfamily rather than 4-hydroxy-2-oxopentanoate (HOPA) aldolase, but it is 
      interesting that the enzyme possesses the activity of HOPA aldolase.
CI  - Copyright (c) 2016 Elsevier Inc. All rights reserved.
FAU - Chen, Qijia
AU  - Chen Q
AD  - National Engineering Laboratory for Industrial Enzymes and Tianjin Engineering 
      Center for Biocatalytic Technology, Tianjin Institute of Industrial 
      Biotechnology, Chinese Academy of Sciences, Tianjin, China; University of Chinese 
      Academy of Sciences, Beijing, China.
FAU - Han, Lei
AU  - Han L
AD  - National Engineering Laboratory for Industrial Enzymes and Tianjin Engineering 
      Center for Biocatalytic Technology, Tianjin Institute of Industrial 
      Biotechnology, Chinese Academy of Sciences, Tianjin, China; University of Chinese 
      Academy of Sciences, Beijing, China.
FAU - Chen, Xi
AU  - Chen X
AD  - National Engineering Laboratory for Industrial Enzymes and Tianjin Engineering 
      Center for Biocatalytic Technology, Tianjin Institute of Industrial 
      Biotechnology, Chinese Academy of Sciences, Tianjin, China.
FAU - Cui, Yunfeng
AU  - Cui Y
AD  - National Engineering Laboratory for Industrial Enzymes and Tianjin Engineering 
      Center for Biocatalytic Technology, Tianjin Institute of Industrial 
      Biotechnology, Chinese Academy of Sciences, Tianjin, China.
FAU - Feng, Jinhui
AU  - Feng J
AD  - National Engineering Laboratory for Industrial Enzymes and Tianjin Engineering 
      Center for Biocatalytic Technology, Tianjin Institute of Industrial 
      Biotechnology, Chinese Academy of Sciences, Tianjin, China.
FAU - Wu, Qiaqing
AU  - Wu Q
AD  - National Engineering Laboratory for Industrial Enzymes and Tianjin Engineering 
      Center for Biocatalytic Technology, Tianjin Institute of Industrial 
      Biotechnology, Chinese Academy of Sciences, Tianjin, China.
FAU - Zhu, Dunming
AU  - Zhu D
AD  - National Engineering Laboratory for Industrial Enzymes and Tianjin Engineering 
      Center for Biocatalytic Technology, Tianjin Institute of Industrial 
      Biotechnology, Chinese Academy of Sciences, Tianjin, China; University of Chinese 
      Academy of Sciences, Beijing, China. Electronic address: zhu_dm@tib.cas.cn.
LA  - eng
PT  - Journal Article
DEP - 20160710
PL  - United States
TA  - Enzyme Microb Technol
JT  - Enzyme and microbial technology
JID - 8003761
RN  - 0 (Bacterial Proteins)
RN  - 0 (Recombinant Proteins)
RN  - EC 4.1.2.- (4-hydroxy-2-ketopentanoic acid aldolase)
RN  - EC 4.1.2.- (Aldehyde-Lyases)
RN  - EC 4.1.3.- (Oxo-Acid-Lyases)
RN  - EC 4.1.3.3 (N-acetylneuraminate lyase)
SB  - IM
MH  - Aldehyde-Lyases/chemistry/genetics/*metabolism
MH  - Amino Acid Sequence
MH  - Bacterial Proteins/chemistry/genetics/*metabolism
MH  - Clostridiales/*enzymology/genetics
MH  - Escherichia coli/enzymology/genetics
MH  - Kinetics
MH  - Oxo-Acid-Lyases/chemistry/genetics/*metabolism
MH  - Recombinant Proteins/chemistry/genetics/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Substrate Specificity
OTO - NOTNLM
OT  - 4-Hydroxy-2-oxopentanoate aldolase
OT  - Aldol addition reaction
OT  - Peptoclostridium difficile
OT  - Sialic acid aldolase
EDAT- 2016/08/21 06:00
MHDA- 2017/05/10 06:00
CRDT- 2016/08/21 06:00
PHST- 2016/03/17 00:00 [received]
PHST- 2016/06/28 00:00 [revised]
PHST- 2016/07/08 00:00 [accepted]
PHST- 2016/08/21 06:00 [entrez]
PHST- 2016/08/21 06:00 [pubmed]
PHST- 2017/05/10 06:00 [medline]
AID - S0141-0229(16)30132-6 [pii]
AID - 10.1016/j.enzmictec.2016.07.003 [doi]
PST - ppublish
SO  - Enzyme Microb Technol. 2016 Oct;92:99-106. doi: 10.1016/j.enzmictec.2016.07.003. 
      Epub 2016 Jul 10.