NDLI: Dye-linked l-malate dehydrogenase from thermophilic Bacillus species DSM 465. Purification and characterization

Please wait, while we are loading the content...

Dye-linked l-malate dehydrogenase from thermophilic Bacillus species DSM 465. Purification and characterization

Content Provider	Scilit
Author	Ohshima, Toshihisa Tanaka, Satohiro
Copyright Year	1993
Description	Journal: Journal of Biological Inorganic Chemistry The distribution of dye‐linked l‐malate dehydrogenase (l‐malate: acceptor oxidoreductase, EC 1.1.99.16) was investigated in many thermophilic bacteria. The enzyme occurred widely in thermophilic spore‐forming bacteria like bacilli and thermoactinomycetes. The enzyme was purified to homogeneity from a thermophile, Bacillus sp. DSM 465, with a 2.7% overall recovery by DEAE‐Toyopearl column chromatography, Sephacryl S‐400 column chromatography and preparative slab PAGE. The enzyme had a molecular mass of about 660 kDa and consisted of about ten subunits all with a molecular mass of 66 kDa. The enzyme retained its full activity upon heating at 55°C for at least 60 min and with incubation at pH 5.0–10.0, 55°C, for 10 min. The enzyme exclusively catalyzed l‐malate dehydrogenation in the presence of an electron acceptor such as 2,6‐dichloroindophenol. The Michaelis constants for l‐malate and 2,6‐dichloroindophenol were determined to be 1.67 mM and 0.050 mM, respectively. FAD was identified as a prosthetic group of the enzyme by HPLC.
Related Links	https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1993.tb17893.x
Ending Page	42
Page Count	6
Starting Page	37
ISSN	09498257
e-ISSN	14321327
DOI	10.1111/j.1432-1033.1993.tb17893.x
Journal	Journal of Biological Inorganic Chemistry
Issue Number	1
Volume Number	214
Language	English
Publisher	Wiley-Blackwell
Publisher Date	1993-05-01
Access Restriction	Open
Subject Keyword	Journal: Journal of Biological Inorganic Chemistry Biotechnology and Microbiology Malate Dehydrogenase Column Chromatography
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Thermostable alanine dehydrogenase from thermophilic Bacillus sphaericus DSM 462. Purification, characterization and kinetic mechanism

Mitochondrial malate dehydrogenase from the thermophilic, filamentous fungus Talaromyces emersonii

Properties and primary structure of the L-malate dehydrogenase from the extremely thermophilic archaebacterium Methanothermus fervidus

Catalytic properties of thermophilic lactate dehydrogenase and halophilic malate dehydrogenase at high temperature and low water activity

Phenylalanine dehydrogenase of Bacillus badius. Purification, characterization and gene cloning

Biochemical and genetic characterization of the membrane-associated malate dehydrogenase (acceptor) from Corynebacterium glutamicum.

Simultaneous purification of L-malate dehydrogenase and L-lactate dehydrogenase from bovine heart by biomimetic-dye affinity chromatography

Purification, characterization and redox properties of hydrogenase from Methanosarcina barkeri (DSM 800)

Purification and characterization of a novel FMN-dependent enzyme. Membrane-bound L-(+)-pantoyl lactone dehydrogenase from Nocardia asteroides

Dye-linked l-malate dehydrogenase from thermophilic Bacillus species DSM 465. Purification and characterization

Similar Documents

Thermostable alanine dehydrogenase from thermophilic Bacillus sphaericus DSM 462. Purification, characterization and kinetic mechanism

Mitochondrial malate dehydrogenase from the thermophilic, filamentous fungus Talaromyces emersonii

Properties and primary structure of the L-malate dehydrogenase from the extremely thermophilic archaebacterium Methanothermus fervidus

Catalytic properties of thermophilic lactate dehydrogenase and halophilic malate dehydrogenase at high temperature and low water activity

Phenylalanine dehydrogenase of Bacillus badius. Purification, characterization and gene cloning

Biochemical and genetic characterization of the membrane-associated malate dehydrogenase (acceptor) from Corynebacterium glutamicum.

Simultaneous purification of L-malate dehydrogenase and L-lactate dehydrogenase from bovine heart by biomimetic-dye affinity chromatography

Purification, characterization and redox properties of hydrogenase from Methanosarcina barkeri (DSM 800)

Purification and characterization of a novel FMN-dependent enzyme. Membrane-bound L-(+)-pantoyl lactone dehydrogenase from Nocardia asteroides

Dye-linked l-malate dehydrogenase from thermophilic Bacillus species DSM 465. Purification and characterization