Identification of Acceptor Substrate Binding Subsites +2 and +3 in the Amylomaltase From Thermus Thermophilus HB8

doi 10.1021/bi602408j.s002
Full Text
Abstract

Available in full text

Date

Unknown

Authors

Unknown

Publisher

American Chemical Society (ACS)

Related search

Simultaneous Polyhydroxyalkanoates and Rhamnolipids Production by Thermus Thermophilus HB8

AMB Express
Applied MicrobiologyBiotechnologyBiophysics
2011English

2P011 Crystal Structure of 4-Oxalocrotonate Tautomerase From Thermus Thermophilus HB8

Seibutsu Butsuri
2004English

Nuclease TT1 From Thermus Thermophilus HB8 Has an Endonuclease Activity Preferential to Circular DNAs

Nucleic Acids Research
Genetics
1980English

The Role of Ribonucleases in Regulating Global mRNA Levels in the Model Organism Thermus Thermophilus HB8

BMC Genomics
BiotechnologyGenetics
2014English

Processing and Termination of 23S rRNA-5S rRNA-tRNA(Gly) Primary Transcripts in Thermus Thermophilus HB8.

Journal of Bacteriology
MicrobiologyMolecular Biology
1991English

Identification and Characterization of Preferred DNA-binding Sites for the Thermus Thermophilus Transcriptional Regulator FadR

PLoS ONE
Multidisciplinary
2017English

Two Nitrate/Nitrite Transporters Are Encoded Within the Mobilizable Plasmid for Nitrate Respiration of Thermus Thermophilus HB8

Journal of Bacteriology
MicrobiologyMolecular Biology
2000English

Characterization of the Nitric Oxide Reductase From Thermus Thermophilus

Proceedings of the National Academy of Sciences of the United States of America
Multidisciplinary
2013English

The Acceptor Specificity of Amylomaltase From Escherichia Coli IFO 3806.

Agricultural and Biological Chemistry
1989English

Amanote Research

Note-taking for researchers

Follow Amanote

© 2024 Amaplex Software S.P.R.L. All rights reserved.

Privacy PolicyRefund Policy