SorF: A Glycosyltransferase With Promiscuous Donor Substrate Specificity in vitro

ChemBioChem ◽  
2007 ◽  
Vol 8 (7) ◽  
pp. 813-819 ◽  
Author(s):  
Maren Kopp ◽  
Carsten Rupprath ◽  
Herbert Irschik ◽  
Andreas Bechthold ◽  
Lothar Elling ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Donor Substrate

scholarly journals Characterization of Phospholipase Activity of the Pseudomonas aeruginosa Type III Cytotoxin, ExoU

2005 ◽  
Vol 187 (3) ◽  
pp. 1192-1195 ◽  
Author(s):  
Hiromi Sato ◽  
Jimmy B. Feix ◽  
Cecilia J. Hillard ◽  
Dara W. Frank
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Substrate Specificity ◽  
Yeast Extract ◽  
Enzyme Activation ◽  
Phospholipase Activity ◽  
Eukaryotic Protein ◽  
Type Iii

ABSTRACT Recombinant ExoU (rExoU) and yeast extract were used to optimize an in vitro phospholipase assay as a basis for identifying the mechanism for enzyme activation and substrate specificity. Our results support a model in which a eukaryotic protein cofactor or complex facilitates the interaction of rExoU with phospholipid substrates.

scholarly journals The in vivo and in vitro substrate specificity of quinoprotein glucose dehydrogenase ofAcinetobacter calcoaceticusLMD79.41

1987 ◽  
Vol 43 (2) ◽  
pp. 195-200 ◽  
Author(s):  
P. Dokter ◽  
J.T. Pronk ◽  
B.J. Schie ◽  
J.P. Dijken ◽  
J.A. Duine
Keyword(s):  
Substrate Specificity ◽  
Glucose Dehydrogenase

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.

Substrate specificity of iodothyronine 5′-deiodinase in rat liver homogenates and its requirements of divalent cations in vitro

Life Sciences ◽  
1986 ◽  
Vol 38 (24) ◽  
pp. 2231-2238 ◽  
Author(s):  
Shinya Kobayshi ◽  
Yan Gao ◽  
Richard L. Ong ◽  
Constance S. Pittman
Keyword(s):  
Substrate Specificity ◽  
Rat Liver ◽  
Divalent Cations ◽  
Liver Homogenates

Differences in Substrate Specificity between Cdk2-Cyclin A and Cdk2-Cyclin E in Vitro

1995 ◽  
Vol 216 (2) ◽  
pp. 520-525 ◽  
Author(s):  
H. Higashi ◽  
I. Suzukitakahashi ◽  
Y. Taya ◽  
K. Segawa ◽  
S. Nishimura ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Cyclin E ◽  
Cyclin A

scholarly journals Relaxed Substrate Specificity in Qβ Replicase through Long-Term In Vitro Evolution

Life ◽  
2021 ◽  
Vol 12 (1) ◽  
pp. 32
Author(s):  
Kohtoh Yukawa ◽  
Ryo Mizuuchi ◽  
Norikazu Ichihashi
Keyword(s):  
Substrate Specificity ◽  
Early Life ◽  
Evolutionary History ◽  
Rna Replication ◽  
Life Forms ◽  
In Vitro Evolution ◽  
Present Evidence ◽  
Major Transition

A change from RNA- to DNA-based genetic systems is hypothesized as a major transition in the evolution of early life forms. One of the possible requirements for this transition is a change in the substrate specificity of the replication enzyme. It is largely unknown how such changes would have occurred during early evolutionary history. In this study, we present evidence that an RNA replication enzyme that has evolved in the absence of deoxyribonucleotide triphosphates (dNTPs) relaxes its substrate specificity and incorporates labeled dNTPs. This result implies that ancient replication enzymes, which probably evolved in the absence of dNTPs, could have incorporated dNTPs to synthesize DNA soon after dNTPs became available. The transition from RNA to DNA, therefore, might have been easier than previously thought.

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