Site-directed mutagenesis of histidine 69 and glutamic acid 148 alters the ribonuclease activity of pea ABR17 (PR10.4)

Plant Physiology and Biochemistry ◽

10.1016/j.plaphy.2010.10.010 ◽

2011 ◽

Vol 49 (9) ◽

pp. 958-962 ◽

Author(s):

Sowmya Krishnaswamy ◽

Pravas Kumar Baral ◽

Michael N.G. James ◽

Nat N.V. Kav

Keyword(s):

Glutamic Acid ◽

Ribonuclease Activity ◽

Site Directed Mutagenesis ◽

Directed Mutagenesis

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Analysis of an invariant cofactor-protein interaction in thiamin diphosphate-dependent enzymes by site-directed mutagenesis. Glutamic acid 418 in transketolase is essential for catalysis.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)31612-0 ◽

1994 ◽

Vol 269 (51) ◽

pp. 32144-32150

Author(s):

C Wikner ◽

L Meshalkina ◽

U Nilsson ◽

M Nikkola ◽

Y Lindqvist ◽

...

Keyword(s):

Glutamic Acid ◽

Protein Interaction ◽

Site Directed Mutagenesis ◽

Directed Mutagenesis ◽

Thiamin Diphosphate

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A site-directed mutagenesis study on Escherichia coli inorganic pyrophosphatase. Glutamic acid-98 and lysine-104 are important for structural integrity, whereas aspartic acids-97 and -102 are essential for catalytic activity

Biochemistry ◽

10.1021/bi00476a017 ◽

1990 ◽

Vol 29 (24) ◽

pp. 5761-5766 ◽

Author(s):

Reijo Lahti ◽

Katariina Pohjanoksa ◽

Taru Pitkaranta ◽

Pirkko Heikinheimo ◽

Tiina Salminen ◽

...

Keyword(s):

Escherichia Coli ◽

Catalytic Activity ◽

Glutamic Acid ◽

Structural Integrity ◽

Site Directed Mutagenesis ◽

Inorganic Pyrophosphatase ◽

Directed Mutagenesis ◽

A Site ◽

Mutagenesis Study

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Site-directed mutagenesis of histidine 93, aspartic acid 180, glutamic acid 205, histidine 290, and aspartic acid 291 at the active site and tryptophan 279 at the raw starch binding site in barley alpha-amylase 1.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)41554-2 ◽

1993 ◽

Vol 268 (30) ◽

pp. 22480-22484

Author(s):

M Søgaard ◽

A Kadziola ◽

R Haser ◽

B Svensson

Keyword(s):

Glutamic Acid ◽

Binding Site ◽

Aspartic Acid ◽

Active Site ◽

Site Directed Mutagenesis ◽

Alpha Amylase ◽

Directed Mutagenesis ◽

Raw Starch Binding

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Site-directed mutagenesis of active-site-related residues inTorpedoacetylcholinesterase Presence of a glutamic acid in the catalytic triad

FEBS Letters ◽

10.1016/0014-5793(92)80821-w ◽

1992 ◽

Vol 309 (3) ◽

pp. 421-423 ◽

Author(s):

Nathalie Duval ◽

Suzanne Bon ◽

Israel Silman ◽

Joel Sussman ◽

Jean Massoulié

Keyword(s):

Glutamic Acid ◽

Active Site ◽

Catalytic Triad ◽

Site Directed Mutagenesis ◽

Directed Mutagenesis

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The Role for Glutamic Acid at Position 196 in Human Hypoxanthine Phosphoribosyltransferase (HPRT) as Investigated Using Site-Directed Mutagenesis

Nucleosides Nucleotides & Nucleic Acids ◽

10.1080/15257770802146593 ◽

2008 ◽

Vol 27 (6-7) ◽

pp. 894-899 ◽

Author(s):

B. Canyuk ◽

A. E-Wan ◽

W. Keawwijit ◽

T. Nualnoi ◽

L. Sirisatean ◽

...

Keyword(s):

Glutamic Acid ◽

Site Directed Mutagenesis ◽

Directed Mutagenesis ◽

Hypoxanthine Phosphoribosyltransferase

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Site-directed mutagenesis of K396R of the 65 kDa glutamic acid decarboxylase active site obliterates enzyme activity but not antibody binding

FEBS Letters ◽

10.1016/s0014-5793(00)02429-7 ◽

2001 ◽

Vol 488 (3) ◽

pp. 185-189 ◽

Author(s):

Christiane S. Hampe ◽

Lisa P. Hammerle ◽

Alberto Falorni ◽

John Robertson ◽

Åke Lernmark

Keyword(s):

Enzyme Activity ◽

Glutamic Acid ◽

Glutamic Acid Decarboxylase ◽

Active Site ◽

Antibody Binding ◽

Site Directed Mutagenesis ◽

Acid Decarboxylase ◽

Directed Mutagenesis

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Site-directed mutagenesis of the beta subunit of tryptophan synthase from Salmonella typhimurium. Role of active site glutamic acid 350.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(20)89492-7 ◽

1991 ◽

Vol 266 (12) ◽

pp. 7618-7625

Author(s):

A M Kayastha ◽

Y Sawa ◽

S Nagata ◽

E W Miles

Keyword(s):

Glutamic Acid ◽

Salmonella Typhimurium ◽

Active Site ◽

Beta Subunit ◽

Site Directed Mutagenesis ◽

Directed Mutagenesis ◽

Tryptophan Synthase

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Site-directed mutagenesis of rat liver S-adenosylhomocysteinase. Effect of conversion of aspartic acid 244 to glutamic acid on coenzyme binding.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)46194-1 ◽

1990 ◽

Vol 265 (27) ◽

pp. 16102-16107

Author(s):

T Gomi ◽

Y Takata ◽

T Date ◽

M Fujioka ◽

R R Aksamit ◽

...

Keyword(s):

Glutamic Acid ◽

Aspartic Acid ◽

Rat Liver ◽

Site Directed Mutagenesis ◽

Directed Mutagenesis ◽

Coenzyme Binding

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Structure and function of an antifreeze polypeptide from ocean pout, Macrozoarces americanus: role of glutamic acid residues in protein stability and antifreeze activity by site-directed mutagenesis

Protein Engineering Design and Selection ◽

10.1093/protein/4.8.1003 ◽

1991 ◽

Vol 4 (8) ◽

pp. 1003-1008 ◽

Author(s):

Xiaomao Li ◽

Choy L. Hew

Keyword(s):

Glutamic Acid ◽

Protein Stability ◽

Structure And Function ◽

Site Directed Mutagenesis ◽

Directed Mutagenesis ◽

And Function ◽

Antifreeze Activity

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Site-directed mutagenesis of arginine 246, glutamic acid 247, and histidine 248 in the eukaryotic transcription factor S-II.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)38477-7 ◽

1990 ◽

Vol 265 (20) ◽

pp. 11854-11857

Author(s):

N Horikoshi ◽

K Sekimizu ◽

S Natori

Keyword(s):

Transcription Factor ◽

Glutamic Acid ◽

Site Directed Mutagenesis ◽

Directed Mutagenesis ◽

Eukaryotic Transcription

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