PMID- 33624365
OWN - NLM
STAT- MEDLINE
DCOM- 20220421
LR  - 20220421
IS  - 1470-8744 (Electronic)
IS  - 0885-4513 (Linking)
VI  - 69
IP  - 2
DP  - 2022 Apr
TI  - Structural and functional diversity of asparaginases: Overview and 
      recommendations for a revised nomenclature.
PG  - 503-513
LID - 10.1002/bab.2127 [doi]
AB  - Asparaginases (ASNases) are a large and structurally diverse group of enzymes 
      ubiquitous amongst archaea, bacteria and eukaryotes, that catalyze hydrolysis of 
      asparagine to aspartate and ammonia. Bacterial ASNases are important 
      biopharmaceuticals for the treatment of acute lymphoblastic leukemia, although 
      some patients experience adverse allergic side effects during treatment with 
      these protein therapeutics. ASNases are currently divided into three families: 
      plant-type ASNases, Rhizobium etli-type ASNases and bacterial-type ASNases. This 
      system is outdated as both bacterial-type and plant-type families also include 
      archaeal, bacterial and eukaryotic enzymes, each with their own distinct 
      characteristics. Herein, phylogenetic studies allied to tertiary structural 
      analyses are described with the aim of proposing a revised and more robust 
      classification system that considers the biochemical diversity of ASNases. 
      Accordingly, based on distinct peptide domains, phylogenetic data, structural 
      analysis and functional characteristics, we recommend that ASNases now be divided 
      into three new distinct classes containing subgroups according to structural and 
      functional aspects. Using this new classification scheme, 25 ASNases were 
      identified as candidates for future new lead discovery.
CI  - (c) 2021 The Authors. Biotechnology and Applied Biochemistry published by Wiley 
      Periodicals LLC on behalf of International Union of Biochemistry and Molecular 
      Biology.
FAU - da Silva, Leonardo Schultz
AU  - da Silva LS
AD  - Instituto de Biociencias, Universidade Estadual Paulista (UNESP), Sao Vicente, 
      Sao Paulo, Brazil.
AD  - Institute of Pharmaceutical Science, School of Cancer & Pharmaceutical Sciences, 
      Faculty of Life Sciences & Medicine, King's College London, UK.
FAU - Doonan, Liam B
AU  - Doonan LB
AD  - Institute of Pharmaceutical Science, School of Cancer & Pharmaceutical Sciences, 
      Faculty of Life Sciences & Medicine, King's College London, UK.
FAU - Pessoa, Adalberto Jr
AU  - Pessoa A Jr
AD  - Departamento de Tecnologia Tecnologia Bioquimico-Farmaceuticas, Faculdade de 
      Ciencias Farmaceuticas, Universidade de Sao Paulo, Sao Paulo, Sao Paulo, Brazil.
FAU - de Oliveira, Marcos Antonio
AU  - de Oliveira MA
AD  - Instituto de Biociencias, Universidade Estadual Paulista (UNESP), Sao Vicente, 
      Sao Paulo, Brazil.
FAU - Long, Paul F
AU  - Long PF
AUID- ORCID: 0000-0001-6698-4602
AD  - Institute of Pharmaceutical Science, School of Cancer & Pharmaceutical Sciences, 
      Faculty of Life Sciences & Medicine, King's College London, UK.
AD  - Departamento de Tecnologia Tecnologia Bioquimico-Farmaceuticas, Faculdade de 
      Ciencias Farmaceuticas, Universidade de Sao Paulo, Sao Paulo, Sao Paulo, Brazil.
LA  - eng
PT  - Journal Article
DEP - 20210319
PL  - United States
TA  - Biotechnol Appl Biochem
JT  - Biotechnology and applied biochemistry
JID - 8609465
RN  - EC 3.5.1.1 (Asparaginase)
SB  - IM
MH  - *Asparaginase/chemistry
MH  - Bacteria/metabolism
MH  - Humans
MH  - Hydrolysis
MH  - Phylogeny
MH  - *Precursor Cell Lymphoblastic Leukemia-Lymphoma
OTO - NOTNLM
OT  - biopharmaceuticals
OT  - bioprospecting
OT  - classification
OT  - enzyme diversity
OT  - l-asparaginase
OT  - phylogeny
EDAT- 2021/02/25 06:00
MHDA- 2022/04/22 06:00
CRDT- 2021/02/24 05:49
PHST- 2020/09/02 00:00 [received]
PHST- 2021/02/09 00:00 [accepted]
PHST- 2021/02/25 06:00 [pubmed]
PHST- 2022/04/22 06:00 [medline]
PHST- 2021/02/24 05:49 [entrez]
AID - 10.1002/bab.2127 [doi]
PST - ppublish
SO  - Biotechnol Appl Biochem. 2022 Apr;69(2):503-513. doi: 10.1002/bab.2127. Epub 2021 
      Mar 19.