2014
DOI: 10.1016/j.bcp.2013.10.001
|View full text |Cite
|
Sign up to set email alerts
|

N-Glycosylation during translation is essential for human arylacetamide deacetylase enzyme activity

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

3
9
0

Year Published

2015
2015
2021
2021

Publication Types

Select...
8

Relationship

1
7

Authors

Journals

citations
Cited by 11 publications
(12 citation statements)
references
References 35 publications
3
9
0
Order By: Relevance
“…However, the glycosylation seemed to affect the activity of the enzymes, and the enzymatic activity of the recombinant proteins was decreased after deglycosylation (Fig 3). This finding is consistent with previous studies showing that glycosylation is required for the full activity of a wide variety of enzymes [31, 32]. The influence of glycosylation on protein properties may be attributed to several functions such as ensuring correct protein folding, preventing proteolytic degradation, and facilitating intracellular transportation [31].…”
Section: Resultssupporting
confidence: 92%
See 1 more Smart Citation
“…However, the glycosylation seemed to affect the activity of the enzymes, and the enzymatic activity of the recombinant proteins was decreased after deglycosylation (Fig 3). This finding is consistent with previous studies showing that glycosylation is required for the full activity of a wide variety of enzymes [31, 32]. The influence of glycosylation on protein properties may be attributed to several functions such as ensuring correct protein folding, preventing proteolytic degradation, and facilitating intracellular transportation [31].…”
Section: Resultssupporting
confidence: 92%
“…This finding is consistent with previous studies showing that glycosylation is required for the full activity of a wide variety of enzymes [31, 32]. The influence of glycosylation on protein properties may be attributed to several functions such as ensuring correct protein folding, preventing proteolytic degradation, and facilitating intracellular transportation [31]. Moreover, glycosylation is one of the greatest advantages of the yeast expression systems [25, 26].…”
Section: Resultssupporting
confidence: 91%
“…Univariable Cox regression analysis, lasso-penalized Cox regression analysis, and multivariable Cox analysis suggested that five SRGs [AADAC (P = 0.008), DEF8 (P = 0.026), HIST1H1C(P = 0.031, MET(P = 0.001), and CHFR(P = 0.041)] were significantly associated with the prognosis of resectable PC,. The arylacetamide deacetylase gene (AADAC) lies on chromosome 3q25.1, and its expressed protein consists of 399 amino acids [34,35]. The protein coded by AADAC protein is extensively implicated in the hydrolysis of various drugs [36], whose function may be related to chemotherapy resistance in pancreatic cancer.…”
Section: Discussionmentioning
confidence: 99%
“…Similar promotional effects were also observed in several related biocatalysts that modified GlcNAc-6-phosphate to GlcN-6-Phosphate. Anderson and his colleagues used the method to make glucosamine fungal as a microbial biomass resource (Scheme 4) [63].…”
Section: Biocatalytic Potential Of Enzymes Involved the Modification Of Glucosamine In Chemotherapeuticalmentioning
confidence: 99%