PMID- 36197832
OWN - NLM
STAT- MEDLINE
DCOM- 20221024
LR  - 20230123
IS  - 2161-5063 (Electronic)
IS  - 2161-5063 (Linking)
VI  - 11
IP  - 10
DP  - 2022 Oct 21
TI  - Interaction between the Anchoring Domain of A-Kinase Anchoring Proteins and the 
      Dimerization and Docking Domain of Protein Kinase A: A Potent Tool for Synthetic 
      Biology.
PG  - 3154-3162
LID - 10.1021/acssynbio.2c00443 [doi]
AB  - Nature is enriched with specific interactions between receptor proteins and their 
      cognate ligands. These interacting pairs can be exploited and applied for the 
      construction of well-ordered multicomponent assemblies with multivalency and 
      multifunctionality. One of the research hotspots of this area is the formation of 
      multienzyme complexes with stable and tunable architectures, which may bear the 
      potential to facilitate cascade biocatalysis and/or strengthen metabolic fluxes. 
      Here we focus on a special interacting pair, the anchoring domain (AD) derived 
      from A-kinase anchoring protein and its interacting dimerization and docking 
      domain (DDD) derived from cyclic AMP-dependent protein kinase, which has 
      potential to be an effective and powerful synthetic biology tool for the 
      construction of multienzyme assemblies. We review the origin and interaction 
      mechanism of AD-DDD, followed by the application of this so-called dock-and-lock 
      pair to form various bioconjugates with multivalency and multispecificity. Then 
      several recent studies related to the construction of multienzyme complexes using 
      AD-DDD, and more specifically, the RIAD-RIDD interacting pair, are presented. 
      Finally, we also discuss the great biotechnology potential and perspectives of 
      AD-DDD as a potent synthetic biology tool for post-translational modifications.
FAU - Wan, Li
AU  - Wan L
AD  - State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, 
      Jiangsu 214122, China.
FAU - Chen, Roulin
AU  - Chen R
AD  - State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, 
      Jiangsu 214122, China.
FAU - Zhu, Yingying
AU  - Zhu Y
AD  - State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, 
      Jiangsu 214122, China.
FAU - Zhang, Wenli
AU  - Zhang W
AUID- ORCID: 0000-0002-7861-0170
AD  - State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, 
      Jiangsu 214122, China.
FAU - Mu, Wanmeng
AU  - Mu W
AUID- ORCID: 0000-0001-6597-527X
AD  - State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, 
      Jiangsu 214122, China.
AD  - International Joint Laboratory on Food Safety, Jiangnan University, Wuxi, Jiangsu 
      214122, China.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20221005
PL  - United States
TA  - ACS Synth Biol
JT  - ACS synthetic biology
JID - 101575075
RN  - 0 (A Kinase Anchor Proteins)
RN  - EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases)
RN  - 0 (Ligands)
RN  - 0 (Multienzyme Complexes)
SB  - IM
MH  - *A Kinase Anchor Proteins/metabolism
MH  - *Cyclic AMP-Dependent Protein Kinases/metabolism
MH  - Dimerization
MH  - Synthetic Biology
MH  - Ligands
MH  - Multienzyme Complexes/metabolism
OTO - NOTNLM
OT  - dock and lock
OT  - metabolic flux control
OT  - multienzyme complexes
OT  - synthetic biology
EDAT- 2022/10/06 06:00
MHDA- 2022/10/25 06:00
CRDT- 2022/10/05 13:13
PHST- 2022/10/06 06:00 [pubmed]
PHST- 2022/10/25 06:00 [medline]
PHST- 2022/10/05 13:13 [entrez]
AID - 10.1021/acssynbio.2c00443 [doi]
PST - ppublish
SO  - ACS Synth Biol. 2022 Oct 21;11(10):3154-3162. doi: 10.1021/acssynbio.2c00443. 
      Epub 2022 Oct 5.