scholarly journals Deacylation of Calcium‐Dependent Antibiotics from Streptomyces violaceoruber in Co‐culture with Streptomyces sp. MG7‐G1

ChemBioChem ◽  
2020 ◽  
Vol 21 (21) ◽  
pp. 3151-3157
Author(s):  
Kathrin Schindl ◽  
Deepika Sharma ◽  
Dieter Spiteller
Keyword(s):  
Streptomyces Sp ◽  
Calcium Dependent ◽  
Streptomyces Violaceoruber

scholarly journals Evidence for an essential histidine residue in d-xylose isomerases

1988 ◽  
Vol 250 (1) ◽  
pp. 153-160 ◽  
Author(s):  
W Vangrysperre ◽  
M Callens ◽  
H Kersters-Hilderson ◽  
C K De Bruyne
Keyword(s):  
Xylose Isomerase ◽  
Lactobacillus Brevis ◽  
Histidine Residue ◽  
Difference Spectra ◽  
Streptomyces Sp ◽  
Histidine Residues ◽  
Tyrosine Residues ◽  
Diethyl Pyrocarbonate ◽  
The Difference ◽  
Streptomyces Violaceoruber

Diethyl pyrocarbonate inactivated D-xylose isomerases from Streptomyces violaceoruber, Streptomyces sp., Lactobacillus xylosus and Lactobacillus brevis with second-order rate constants of 422, 417, 99 and 92 M-1.min-1 respectively (at pH 6.0 and 25 degrees C). Activity was completely restored by the addition of neutral hydroxylamine, and total protection was afforded by the substrate analogue xylitol in the presence of either Mg2+ or Mn2+ according to the genus studied. The difference spectra of the modified enzymes revealed an absorption maximum at 237-242 nm, characteristic for N-ethoxycarbonylhistidine. In addition, the spectrum of ethoxycarbonylated D-xylose isomerase from L. xylosus showed absorption minima at both 280 and 230 nm, indicative for modification of tyrosine residues. Nitration with tetranitromethane followed by diethyl pyrocarbonate treatment eliminated the possibility that modification of tyrosine residues was responsible for inactivation, and resulted in modification of one non-essential tyrosine residue and six histidine residues. Inactivation of the other D-xylose isomerases with diethyl pyrocarbonate required the modification of one (L. brevis), two (Streptomyces sp.) and four (S. violaceoruber) histidine residues per monomer. Spectral analysis and maintenance of total enzyme activities further indicated that either xylitol Mg2+ (streptomycetes) or xylitol Mn2+ (lactobacilli) prevented the modification of one crucial histidine residue. The overall results thus provide evidence that a single active-site histidine residue is involved in the catalytic reaction mechanism of D-xylose isomerases.

scholarly journals Reaction of Woodward's reagent K with d-xylose isomerases. Modification of an active site carboxylate residue

1989 ◽  
Vol 260 (1) ◽  
pp. 163-169 ◽  
Author(s):  
W Vangrysperre ◽  
H Kersters-Hilderson ◽  
M Callens ◽  
C K De Bruyne
Keyword(s):  
Spectral Analysis ◽  
Catalytic Activity ◽  
Active Site ◽  
Rate Constants ◽  
Bacillus Coagulans ◽  
Lactobacillus Brevis ◽  
Carboxylate Group ◽  
Streptomyces Sp ◽  
Woodward’S Reagent K ◽  
Streptomyces Violaceoruber

D-Xylose isomerases from Streptomyces violaceoruber, Streptomyces sp., Lactobacillus xylosus, Lactobacillus brevis and Bacillus coagulans were rapidly inactivated by Woodward's reagent K. Second-order rate constants in the absence of ligands, at pH 6.0 and 25 degrees C, were 41, 36, 22, 95 and 26 M-1.min-1 respectively. Spectral analysis at 340 nm revealed that inactivation was correlated with modification of five, six, two, three and six carboxylate residues per monomer respectively. In the presence of protecting ligands, modification of one carboxylate group was prevented. The results support the idea of an active site glutamate or aspartate group that may contribute to the catalytic activity of all these D-xylose isomerases.

Genomic analysis of C-type lectins

2002 ◽  
Vol 69 ◽  
pp. 59-72 ◽  
Author(s):  
Kurt Drickamer ◽  
Andrew J. Fadden
Keyword(s):  
Biological Effects ◽  
Cell Signalling ◽  
Genomic Analysis ◽  
Binding Activity ◽  
Immunoglobulin Superfamily ◽  
Carbohydrate Binding ◽  
Carbohydrate Recognition ◽  
Calcium Dependent ◽  
Binding Domains ◽  
Carbohydrate Recognition Domains

Many biological effects of complex carbohydrates are mediated by lectins that contain discrete carbohydrate-recognition domains. At least seven structurally distinct families of carbohydrate-recognition domains are found in lectins that are involved in intracellular trafficking, cell adhesion, cell–cell signalling, glycoprotein turnover and innate immunity. Genome-wide analysis of potential carbohydrate-binding domains is now possible. Two classes of intracellular lectins involved in glycoprotein trafficking are present in yeast, model invertebrates and vertebrates, and two other classes are present in vertebrates only. At the cell surface, calcium-dependent (C-type) lectins and galectins are found in model invertebrates and vertebrates, but not in yeast; immunoglobulin superfamily (I-type) lectins are only found in vertebrates. The evolutionary appearance of different classes of sugar-binding protein modules parallels a development towards more complex oligosaccharides that provide increased opportunities for specific recognition phenomena. An overall picture of the lectins present in humans can now be proposed. Based on our knowledge of the structures of several of the C-type carbohydrate-recognition domains, it is possible to suggest ligand-binding activity that may be associated with novel C-type lectin-like domains identified in a systematic screen of the human genome. Further analysis of the sequences of proteins containing these domains can be used as a basis for proposing potential biological functions.

Antifungal alkaloids from Agelas Citrina that decouple calcium-dependent excitation-contraction

Planta Medica ◽  
2012 ◽  
Vol 78 (11) ◽  
Author(s):  
TF Molinski ◽  
EP Stout ◽  
LCY Yu ◽  
KM Truong ◽  
IN Pessah
Keyword(s):  
Calcium Dependent

Calcium-dependent release of adipocyte fatty acid binding protein from human adipocytes

2014 ◽  
Vol 122 (03) ◽  
Author(s):  
I Schlottmann ◽  
M Ehrhart-Bornstein ◽  
M Wabitsch ◽  
SR Bornstein ◽  
V Lamounier-Zepter
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Human Adipocytes ◽  
Fatty Acid Binding ◽  
Calcium Dependent ◽  
Acid Binding Protein

Structure determination and biosynthesis of the antifungal butyrolactols from Streptomyces sp.

Planta Medica ◽  
2016 ◽  
Vol 81 (S 01) ◽  
pp. S1-S381 ◽  
Author(s):  
K Ko ◽  
HM Ge ◽  
J Shin ◽  
DC Oh
Keyword(s):  
Structure Determination ◽  
Streptomyces Sp

Glycoproteins IIb and IIIa and Platelet Thrombospondin in a Liposome Model of Platelet Aggregation

1986 ◽  
Vol 55 (02) ◽  
pp. 240-245 ◽  
Author(s):  
M E Rybak
Keyword(s):  
Platelet Aggregation ◽  
Direct Evidence ◽  
Phospholipid Vesicles ◽  
Aggregate Formation ◽  
Membrane Glycoproteins ◽  
Protein Orientation ◽  
Phosphatidylcholine Liposomes ◽  
Calcium Dependent ◽  
Lentil Lectin ◽  
Complete Reversal

SummaryPlatelet membrane glycoproteins IIb and IIIa and platelet thrombospondin were incorporated onto phosphatidylcholine liposomes, by freeze thawing and sonication. Protein orientation on the liposomes was confirmed by susceptibility to neuraminidase cleavage and binding to lentil lectin-Sepharose (GPIIb-IIIa liposomes) and to heparin-Sepharose (thrombospondin liposomes). Glycoproteins Ilb-IIIa bound 125I-fibrinogen with Kd of 7.5 × 10™7M. Binding was reversible and calcium-dependent. Ilb-IIIa liposomes underwent fibrinogen-dependent aggregation in the presence of 10 mM CaCl2. Maximal aggregate formation was observed with a combination of IIb-IIIa liposomes and thrombospondin liposomes. This aggregation was partially inhibited by preincubation with monoclonal antibodies to the IIb-IIIa complex. Addition of EDTA caused complete reversal of aggregates. Thrombospondin liposomes also underwent fibrinogen and calcium dependent aggregation, however, this aggregation was less than that observed with the GPIIb-IIIa liposomes. Maximal aggregate formation was observed with a mixture of IIb-IIIa liposomes and thrombospondin liposomes. These studies demonstrate that GPIIb-IIIa and thrombospondin can be incorporated into phospholipid vesicles with preservation of function. Direct evidence is provided to demonstrate that glycoprotein lib and Ilia and fibrinogen are sufficient for platelet aggregation and to demonstrate that thrombospondin may also contribute to platelet aggregation.

Calcium-Dependent Protein Kinases (CDPK) in Abiotic Stress Tolerance

2018 ◽  
Vol 34 (2) ◽  
pp. 259-265 ◽  
Author(s):  
Hemant B Kardile ◽  
◽  
Vikrant ◽  
Nirmal Kant Sharma ◽  
Ankita Sharma ◽  
...  
Keyword(s):  
Abiotic Stress ◽  
Stress Tolerance ◽  
Protein Kinases ◽  
Abiotic Stress Tolerance ◽  
Calcium Dependent ◽  
Dependent Protein ◽  
Calcium Dependent Protein Kinases

Exemplar Abstract for Streptomyces sp. None 2015.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Dorothea Taylor ◽  
George M Garrity
Keyword(s):  
Streptomyces Sp

Exemplar Abstract for Streptomyces sp. None 2015.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Dorothea Taylor ◽  
George M Garrity
Keyword(s):  
Streptomyces Sp
Sign in / Sign up

Export Citation Format

Share Document