NDLI: Alkaline phosphatase from the hyperthermophilic bacterium T. maritima requires cobalt for activity.

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

Year: 2017 Volume: 26

Year: 2016 Volume: 25

Year: 2015 Volume: 24

Year: 2014 Volume: 23

Year: 2013 Volume: 22

Year: 2012 Volume: 21

Year: 2011 Volume: 20

Year: 2010 Volume: 19

Year: 2009 Volume: 18

Year: 2008 Volume: 17

Year: 2007 Volume: 16

Year: 2006 Volume: 15

Year: 2005 Volume: 14

Year: 2004 Volume: 13

Year: 2003 Volume: 12

Year: 2002 Volume: 11

Year: 2002 Volume: 11 Issue: 12

Year: 2002 Volume: 11 Issue: 11

Year: 2002 Volume: 11 Issue: 10

Year: 2002 Volume: 11 Issue: 9

Year: 2002 Volume: 11 Issue: 8

Year: 2002 Volume: 11 Issue: 7

Year: 2002 Volume: 11 Issue: 6

Year: 2002 Volume: 11 Issue: 5

Year: 2002 Volume: 11 Issue: 4

Structural genomics: a pipeline for providing structures for the biologist.

Natively unfolded proteins: a point where biology waits for physics.

Histidine pK(a) shifts and changes of tautomeric states induced by the binding of gallium-protoporphyrin IX in the hemophore HasA(SM).

Amino acid intrinsic alpha-helical propensities III: positional dependence at several positions of C terminus.

Fine-tuning function: correlation of hinge domain interactions with functional distinctions between LacI and PurR.

Classification of G-protein coupled receptors by alignment-independent extraction of principal chemical properties of primary amino acid sequences.

Analysis of serine proteinase–inhibitor interaction by alanine shaving

The interdigitated beta-helix domain of the P22 tailspike protein acts as a molecular clamp in trimer stabilization.

Hydroxynonenal inactivates cathepsin B by forming Michael adducts with active site residues.

Thermodynamic stability measurements on multimeric proteins using a new H/D exchange- and matrix-assisted laser desorption/ionization (MALDI) mass spectrometry-based method.

Probability-based protein secondary structure identification using combined NMR chemical-shift data.

Mass spectrometric analysis of the kinetics of in vivo rhodopsin phosphorylation.

Complex behavior in solution of homodimeric SecA.

Improved affinity of engineered streptavidin for the Strep-tag II peptide is due to a fixed open conformation of the lid-like loop at the binding site.

Subunit composition of a bicomponent toxin: staphylococcal leukocidin forms an octameric transmembrane pore.

Alkaline phosphatase from the hyperthermophilic bacterium T. maritima requires cobalt for activity.

Modeling the transmembrane domain of bacterial chemoreceptors.

Thermodynamics of single peptide bond cleavage in bovine pancreatic trypsin inhibitor (BPTI).

Free-thiol Cys331 exposed during activation process is critical for native tetramer structure of cathepsin C (dipeptidyl peptidase I).

Ca(II)- and Tb(III)-induced stabilization and refolding of anticoagulation factor I from the venom of Agkistrodon acutus

Dynamical characterization of residual and non-native structures in a partially folded protein by (15)N NMR relaxation using a model based on a distribution of correlation times.

Direct proton magnetic resonance determination of the pKa of the active center histidine in thiolsubtilisin.

Acyl group specificity at the active site of tetrahydridipicolinate N-succinyltransferase.

Polyproline II helical structure in protein unfolded states: lysine peptides revisited.

Free energies of protein decoys provide insight into determinants of protein stability.

Year: 2002 Volume: 11 Issue: 3

Year: 2002 Volume: 11 Issue: 2

Year: 2002 Volume: 11 Issue: 1

Year: 2001 Volume: 10

Year: 2000 Volume: 9

Year: 1999 Volume: 8

Year: 1998 Volume: 7

Year: 1997 Volume: 6

Year: 1996 Volume: 5

Year: 1995 Volume: 4

Year: 1994 Volume: 3

Year: 1993 Volume: 2

Year: 1992 Volume: 1

Alkaline phosphatase from the hyperthermophilic bacterium T. maritima requires cobalt for activity.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Kantrowitz, Evan R. Cardia, James P. Wojciechowski, Cheryl L.
Description	Country affiliation: United States Author Affiliation: Wojciechowski CL ( Merkert Chemistry Center, Boston College, Chestnut Hill, Massachusetts 02467, USA.)
Abstract	The hyperthermophilic bacterium Thermotoga maritima encodes a gene sharing sequence similarities with several known genes for alkaline phosphatase (AP). The putative gene was isolated and the corresponding protein expressed in Escherichia coli, with and without a predicted signal sequence. The recombinant protein showed phosphatase activity toward the substrate p-nitrophenyl-phosphate with a k(cat) of 16 s(-1) and a K(m) of 175 microM at a pH optimum of 8.0 when assayed at 25 degrees C. T. maritima phosphatase activity increased at high temperatures, reaching a maximum k(cat) of 100 s(-1), with a K(m) of 93 microM at 65 degrees C. Activity was stable at 65 degrees C for >24 h and at 90 degrees C for 5 h. Phosphatase activity was dependent on divalent metal ions, specifically Co(II) and Mg(II). Circular dichroism spectra showed that the enzyme gains secondary structure on addition of these metals. Zinc, the most common divalent metal ion required for activity in known APs, was shown to inhibit the T. maritima phosphatase enzyme at concentrations above 0.3 moles Zn: 1 mole monomer. All activity was abolished in the presence of 0.1 mM EDTA. The T. maritima AP primary sequence is 28% identical when compared with E. coli AP. Based on a structural model, the active sites are superimposable except for two residues near the E. coli AP Mg binding site, D153 and K328 (E. coli numbering) corresponding to histidine and tryptophan in T. maritima AP, respectively. Sucrose-density gradient sedimentation experiments showed that the protein exists in several quaternary forms predominated by an octamer.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	4
Volume Number	11
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2002-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Alkaline Phosphatase Chemistry Cobalt Thermotoga Maritima Enzymology Metabolism Amino Acid Sequence Binding Sites Dna Primers Dimerization Enzyme Stability Escherichia Coli Genetics Hot Temperature Hydrogen-ion Concentration Molecular Sequence Data Plasmids Polymerase Chain Reaction Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

Central Library (ISO-9001:2015 Certified)
Indian Institute of Technology Kharagpur
Kharagpur, West Bengal, India | PIN - 721302

See location in the Map
03222 282435
Mail: support@ndl.gov.in

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