Sequence of GLN1B_MYCTU
EC Number:6.3.1.2
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
Other sequences found for EC No. 6.3.1.2
General information:
Sequence
0 MTEKTPDDVF KLAKDEKVEY VDVRFCDLPG IMQHFTIPAS AFDKSVFDDG LAFDGSSIRG
60 FQSIHESDML LLPDPETARI DPFRAAKTLN INFFVHDPFT LEPYSRDPRN IARKAENYLI
120 STGIADTAYF GAEAEFYIFD SVSFDSRANG SFYEVDAISG WWNTGAATEA DGSPNRGYKV
180 RHKGGYFPVA PNDQYVDLRD KMLTNLINSG FILEKGHHEV GSGGQAEINY QFNSLLHAAD
240 DMQLYKYIIK NTAWQNGKTV TFMPKPLFGD NGSGMHCHQS LWKDGAPLMY DETGYAGLSD
300 TARHYIGGLL HHAPSLLAFT NPTVNSYKRL VPGYEAPINL VYSQRNRSAC VRIPITGSNP
360 KAKRLEFRSP DSSGNPYLAF SAMLMAGLDG IKNKIEPQAP VDKDLYELPP EEAASIPQTP
420 TQLSDVIDRL EADHEYLTEG GVFTNDLIET WISFKRENEI EPVNIRPHPY EFALYYDV
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
297402
Harth G.,Horwitz M.A.
Expression and efficient export of enzymatically active Mycobacterium tuberculosis glutamine synthetase in Mycobacterium smegmatis and evidence that the information for export is contained within the protein.
J. Biol. Chem.
272
22728-22735
1997
297403
Cole S.T.,Brosch R.,Parkhill J.,Garnier T.,Churcher C.M.,Harris D.E.,Gordon S.V.,Eiglmeier K.,Gas S.,Barry C.E. III,Tekaia F.,Badcock K.,Basham D.,Brown D.,Chillingworth T.,Connor R.,Davies R.M.,Devlin K.,Feltwell T.,Gentles S.,Hamlin N.,Holroyd S.,Hornsby T.,Jagels K.,Krogh A.,McLean J.,Moule S.,Murphy L.D.,Oliver S.,Osborne J.,Quail M.A.,Rajandream M.A.,Rogers J.,Rutter S.,Seeger K.,Skelton S.,Squares S.,Squares R.,Sulston J.E.,Taylor K.,Whitehead S.,Barrell B.G.
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
Nature
393
537-544
1998
297404
Harth G.,Clemens D.L.,Horwitz M.A.
Glutamine synthetase of Mycobacterium tuberculosis: extracellular release and characterization of its enzymatic activity.
Proc. Natl. Acad. Sci. U.S.A.
91
9342-9346
1994
297405
Harth G.,Zamecnik P.C.,Tang J.Y.,Tabatadze D.,Horwitz M.A.
Treatment of Mycobacterium tuberculosis with antisense oligonucleotides to glutamine synthetase mRNA inhibits glutamine synthetase activity, formation of the poly-L-glutamate/glutamine cell wall structure, and bacterial replication.
Proc. Natl. Acad. Sci. U.S.A.
97
418-423
2000
297406
Harth G.,Horwitz M.A.
Inhibition of Mycobacterium tuberculosis glutamine synthetase as a novel antibiotic strategy against tuberculosis: demonstration of efficacy in vivo.
Infect. Immun.
71
456-464
2003
297407
Tullius M.V.,Harth G.,Horwitz M.A.
Glutamine synthetase GlnA1 is essential for growth of Mycobacterium tuberculosis in human THP-1 macrophages and guinea pigs.
Infect. Immun.
71
3927-3936
2003
297408
Mehta R.,Pearson J.T.,Mahajan S.,Nath A.,Hickey M.J.,Sherman D.R.,Atkins W.M.
Adenylylation and catalytic properties of Mycobacterium tuberculosis glutamine synthetase expressed in Escherichia coli versus mycobacteria.
J. Biol. Chem.
279
22477-22482
2004
297409
Kelkar D.S.,Kumar D.,Kumar P.,Balakrishnan L.,Muthusamy B.,Yadav A.K.,Shrivastava P.,Marimuthu A.,Anand S.,Sundaram H.,Kingsbury R.,Harsha H.C.,Nair B.,Prasad T.S.,Chauhan D.S.,Katoch K.,Katoch V.M.,Kumar P.,Chaerkady R.,Ramachandran S.,Dash D.,Pandey A.
Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry.
Mol. Cell. Proteomics
10
0-0
2011
297410
Gill H.S.,Pfluegl G.M.,Eisenberg D.
Multicopy crystallographic refinement of a relaxed glutamine synthetase from Mycobacterium tuberculosis highlights flexible loops in the enzymatic mechanism and its regulation.
Biochemistry
41
9863-9872
2002
297411
Krajewski W.W.,Jones T.A.,Mowbray S.L.
Structure of Mycobacterium tuberculosis glutamine synthetase in complex with a transition-state mimic provides functional insights.
Proc. Natl. Acad. Sci. U.S.A.
102
10499-10504
2005
297412
Nilsson M.T.,Krajewski W.W.,Yellagunda S.,Prabhumurthy S.,Chamarahally G.N.,Siddamadappa C.,Srinivasa B.R.,Yahiaoui S.,Larhed M.,Karlen A.,Jones T.A.,Mowbray S.L.
Structural basis for the inhibition of Mycobacterium tuberculosis glutamine synthetase by novel ATP-competitive inhibitors.
J. Mol. Biol.
393
504-513
2009
297413
Gising J.,Nilsson M.T.,Odell L.R.,Yahiaoui S.,Lindh M.,Iyer H.,Sinha A.M.,Srinivasa B.R.,Larhed M.,Mowbray S.L.,Karlen A.
Trisubstituted imidazoles as Mycobacterium tuberculosis glutamine synthetase inhibitors.
J. Med. Chem.
55
2894-2898
2012
