scholarly journals Nudix proteins affecting microbial pathogenesis

Microbiology ◽  
2020 ◽  
Vol 166 (12) ◽  
pp. 1110-1114 ◽  
Author(s):  
Elzbieta Kraszewska ◽  
Joanna Drabinska
Keyword(s):  
Substrate Specificity ◽  
The State ◽  
Microbial Pathogenesis ◽  
Cellular Functions ◽  
Broad Substrate Specificity ◽  
Domains Of Life ◽  
Hydrolysis Of

Nudix proteins catalyse hydrolysis of pyrophosphate bonds in a variety of substrates and are ubiquitous in all domains of life. Their widespread presence and broad substrate specificity suggest that they have important cellular functions. In this review, we summarize the state of knowledge on microbial Nudix proteins involved in pathogenesis.

scholarly journals Purification and Cloning of a Broad Substrate Specificity Human Liver Carboxylesterase That Catalyzes the Hydrolysis of Cocaine and Heroin

1997 ◽  
Vol 272 (23) ◽  
pp. 14769-14775 ◽  
Author(s):  
Evgenia V. Pindel ◽  
Natalia Y. Kedishvili ◽  
Trent L. Abraham ◽  
Monica R. Brzezinski ◽  
Jing Zhang ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Human Liver ◽  
Broad Substrate Specificity ◽  
Hydrolysis Of

scholarly journals Xylanase and Acetyl Xylan Esterase Activities of XynA, a Key Subunit of the Clostridium cellulovorans Cellulosome for Xylan Degradation

2002 ◽  
Vol 68 (12) ◽  
pp. 6399-6402 ◽  
Author(s):  
Akihiko Kosugi ◽  
Koichiro Murashima ◽  
Roy H. Doi
Keyword(s):  
Substrate Specificity ◽  
Glycoside Hydrolase ◽  
Catalytic Domain ◽  
Acetyl Xylan Esterase ◽  
Clostridium Cellulovorans ◽  
Broad Substrate Specificity ◽  
Xylan Degradation ◽  
Hydrolysis Of ◽  
Esterase Activities

ABSTRACT The Clostridium cellulovorans xynA gene encodes the cellulosomal endo-1,4-β-xylanase XynA, which consists of a family 11 glycoside hydrolase catalytic domain (CD), a dockerin domain, and a NodB domain. The recombinant acetyl xylan esterase (rNodB) encoded by the NodB domain exhibited broad substrate specificity and released acetate not only from acetylated xylan but also from other acetylated substrates. rNodB acted synergistically with the xylanase CD of XynA for hydrolysis of acetylated xylan. Immunological analyses revealed that XynA corresponds to a major xylanase in the cellulosomal fraction. These results indicate that XynA is a key enzymatic subunit for xylan degradation in C. cellulovorans.

scholarly journals A corynecaterium glutamicum expression system for glycoside hydrolase analysis

2021 ◽  
Author(s):  
Hirak Saxena
Keyword(s):  
Expression System ◽  
Lysosomal Storage Diseases ◽  
Industrial Applications ◽  
Glycoside Hydrolases ◽  
Cellulosic Biomass ◽  
Lysosomal Storage ◽  
Cellular Functions ◽  
Domains Of Life ◽  
Hydrolysis Of ◽  
Structure And Activity

The biological hydrolysis of glycosidic linkages in complex sugars is facilitated by glycoside hydrolases. These enzymes are ubiquitous across all domains of life, playing significant roles in important biological processes like the degradation of cellulosic biomass, viral pathogenesis, antibacterial defense, and normal cellular functions. The potential industrial applications of highly efficient glycoside hydrolases, as well as the fact that a number of lysosomal storage diseases have been attributed to deficiencies in these enzymes 43, 22, merits further study into their structure and activity. For this reason, a handful of novel glycoside hydrolases from Cellulomonas fimi, a Gram-positive Actinobacteria known for its ability to degrade cellulose 39, will be cloned, expressed and biochemically analyzed.

scholarly journals A corynecaterium glutamicum expression system for glycoside hydrolase analysis

2021 ◽  
Author(s):  
Hirak Saxena
Keyword(s):  
Expression System ◽  
Lysosomal Storage Diseases ◽  
Industrial Applications ◽  
Glycoside Hydrolases ◽  
Cellulosic Biomass ◽  
Lysosomal Storage ◽  
Cellular Functions ◽  
Domains Of Life ◽  
Hydrolysis Of ◽  
Structure And Activity

The biological hydrolysis of glycosidic linkages in complex sugars is facilitated by glycoside hydrolases. These enzymes are ubiquitous across all domains of life, playing significant roles in important biological processes like the degradation of cellulosic biomass, viral pathogenesis, antibacterial defense, and normal cellular functions. The potential industrial applications of highly efficient glycoside hydrolases, as well as the fact that a number of lysosomal storage diseases have been attributed to deficiencies in these enzymes 43, 22, merits further study into their structure and activity. For this reason, a handful of novel glycoside hydrolases from Cellulomonas fimi, a Gram-positive Actinobacteria known for its ability to degrade cellulose 39, will be cloned, expressed and biochemically analyzed.

scholarly journals Carboxylic Ester Hydrolases in Bacteria: Active Site, Structure, Function and Application

Crystals ◽  
2019 ◽  
Vol 9 (11) ◽  
pp. 597 ◽  
Author(s):  
Changsuk Oh ◽  
T. Doohun Kim ◽  
Kyeong Kyu Kim
Keyword(s):  
Acyl Chain ◽  
Data Bank ◽  
Industrial Applications ◽  
Head Group ◽  
Carboxylic Ester ◽  
Site Structure ◽  
Domains Of Life ◽  
Carboxylic Esters ◽  
Hydrolysis Of ◽  
Ester Hydrolases

Carboxylic ester hydrolases (CEHs), which catalyze the hydrolysis of carboxylic esters to produce alcohol and acid, are identified in three domains of life. In the Protein Data Bank (PDB), 136 crystal structures of bacterial CEHs (424 PDB codes) from 52 genera and metagenome have been reported. In this review, we categorize these structures based on catalytic machinery, structure and substrate specificity to provide a comprehensive understanding of the bacterial CEHs. CEHs use Ser, Asp or water as a nucleophile to drive diverse catalytic machinery. The α/β/α sandwich architecture is most frequently found in CEHs, but 3-solenoid, β-barrel, up-down bundle, α/β/β/α 4-layer sandwich, 6 or 7 propeller and α/β barrel architectures are also found in these CEHs. Most are substrate-specific to various esters with types of head group and lengths of the acyl chain, but some CEHs exhibit peptidase or lactamase activities. CEHs are widely used in industrial applications, and are the objects of research in structure- or mutation-based protein engineering. Structural studies of CEHs are still necessary for understanding their biological roles, identifying their structure-based functions and structure-based engineering and their potential industrial applications.

scholarly journals Erratum to: “Self-assembling catalytic systems based on new amphiphile containing purine fragment, exhibiting substrate specificity in hydrolysis of phosphorus acids esters”

2017 ◽  
Vol 87 (7) ◽  
pp. 1649-1649
Author(s):  
D. A. Samarkina ◽  
D. R. Gabdrakhmanov ◽  
V. E. Semenov ◽  
F. G. Valeeva ◽  
L. M. Gubaidullina ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Catalytic Systems ◽  
Self Assembling ◽  
Hydrolysis Of

scholarly journals LASS3 (longevity assurance homologue 3) is a mainly testis-specific (dihydro)ceramide synthase with relatively broad substrate specificity

2006 ◽  
Vol 398 (3) ◽  
pp. 531-538 ◽  
Author(s):  
Yukiko Mizutani ◽  
Akio Kihara ◽  
Yasuyuki Igarashi
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Family Members ◽  
Fatty Acyl ◽  
Ceramide Synthase ◽  
Broad Substrate Specificity ◽  
Acid Protein ◽  
Amino Acid Protein

The LASS (longevity assurance homologue) family members are highly conserved from yeasts to mammals. Five mouse and human LASS family members, namely LASS1, LASS2, LASS4, LASS5 and LASS6, have been identified and characterized. In the present study we cloned two transcriptional variants of hitherto-uncharacterized mouse LASS3 cDNA, which encode a 384-amino-acid protein (LASS3) and a 419-amino-acid protein (LASS3-long). In vivo, [3H]dihydrosphingosine labelling and electrospray-ionization MS revealed that overproduction of either LASS3 isoform results in increases in several ceramide species, with some preference toward those having middle- to long-chain-fatty acyl-CoAs. A similar substrate preference was observed in an in vitro (dihydro)ceramide synthase assay. These results indicate that LASS3 possesses (dihydro)ceramide synthesis activity with relatively broad substrate specificity. We also found that, except for a weak display in skin, LASS3 mRNA expression is limited almost solely to testis, implying that LASS3 plays an important role in this gland.

scholarly journals TheArabidopsisAtSTE24 Is a CAAXProtease with Broad Substrate Specificity

2002 ◽  
Vol 277 (33) ◽  
pp. 29856-29864 ◽  
Author(s):  
Keren Bracha ◽  
Meirav Lavy ◽  
Shaul Yalovsky
Keyword(s):  
Substrate Specificity ◽  
Broad Substrate Specificity
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