Crystal structure of L-lysyl-L-glutamic acid dihydrate

2009 ◽  
Vol 34 (1) ◽  
pp. 42-45 ◽  
Author(s):  
HEMANT P. YENNAWAR ◽  
M.A. VISWAMITRA
Keyword(s):  
Crystal Structure ◽  
Glutamic Acid

Preparation and crystal structure of new samarium complexes with glutamic acid

2003 ◽  
Vol 660 (1-3) ◽  
pp. 99-106 ◽  
Author(s):  
Julia Torres ◽  
Carlos Kremer ◽  
Helena Pardo ◽  
Leopoldo Suescun ◽  
Alvaro Mombrú ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Glutamic Acid ◽  
Samarium Complexes

WHICH IS THE PROTON-SHUTTLE IN ISOXANTHOPTERIN DEAMINASE? QM/MM MD UNDERSTANDING

2013 ◽  
Vol 12 (08) ◽  
pp. 1341002 ◽  
Author(s):  
XIN ZHANG ◽  
MING LEI
Keyword(s):  
Crystal Structure ◽  
Molecular Dynamics ◽  
Hydrogen Bonds ◽  
Proton Transfer ◽  
Glutamic Acid ◽  
Active Site ◽  
Nucleophilic Attack ◽  
Zinc Ions ◽  
Initial Model ◽  
Dynamics Simulations

The deamination process of isoxanthopterin catalyzed by isoxanthopterin deaminase was determined using the combined QM(PM3)/MM molecular dynamics simulations. In this paper, the updated PM3 parameters were employed for zinc ions and the initial model was built up based on the crystal structure. Proton transfer and following steps have been investigated in two paths: Asp336 and His285 serve as the proton shuttle, respectively. Our simulations showed that His285 is more effective than Aap336 in proton transfer for deamination of isoxanthopterin. As hydrogen bonds between the substrate and surrounding residues play a key role in nucleophilic attack, we suggested mutating Thr195 to glutamic acid, which could enhance the hydrogen bonds and help isoxanthopterin get close to the active site. The simulations which change the substrate to pterin 6-carboxylate also performed for comparison. Our results provide reference for understanding of the mechanism of deaminase and for enhancing the deamination rate of isoxanthopterin deaminase.

The crystal structure of L(+)-glutamic acid hydroiodide, l-C5H9NO4 · HI

1985 ◽  
Vol 171 (1-2) ◽  
Author(s):  
A. Kirfel ◽  
F. Wallrafen
Keyword(s):  
Crystal Structure ◽  
Glutamic Acid ◽  
Single Crystal ◽  
Structure Analysis ◽  
X Ray

AbstractSingle crystal X-ray structure analysis shows

Low Temperature Crystal Structure of N-Acetyl-l-Glutamic Acid: Comparison with the DFT Calculated Structure

2010 ◽  
Vol 40 (7) ◽  
pp. 602-607 ◽  
Author(s):  
Nighat Kausar ◽  
Bruce D. Alexander ◽  
Rex A. Palmer ◽  
Brian S. Potter ◽  
Trevor J. Dines ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Low Temperature ◽  
Glutamic Acid ◽  
Low Temperature Crystal Structure ◽  
Acid Comparison

scholarly journals Stabilization of the oxy form of tyrosinase by a single conservative amino acid substitution

1992 ◽  
Vol 282 (3) ◽  
pp. 915-918 ◽  
Author(s):  
M P Jackman ◽  
M Huber ◽  
A Hajnal ◽  
K Lerch
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Glutamic Acid ◽  
Amino Acid Substitution ◽  
Kinetic Properties ◽  
Binding Region ◽  
Invariant Residue ◽  
Streptomyces Glaucescens

Asp-208 of Streptomyces glaucescens tyrosinase (an invariant residue in the CuB-binding region of tyrosinases and haemocyanins) was conservatively substituted by glutamic acid. Although having little effect on spectroscopic or kinetic properties of the enzyme, the mutation greatly decreased the lability of Cu-bound O2. A rationalization for these results is given, based on the crystal structure of Panuliris interruptus haemocyanin in the conserved CuB-binding region.

Crystal structure analysis of a mutant Escherichia coli thioredoxin in which lysine 36 is replaced by glutamic acid

Biochemistry ◽  
1993 ◽  
Vol 32 (19) ◽  
pp. 5093-5098 ◽  
Author(s):  
Matti Nikkola ◽  
Florence K. Gleason ◽  
James A. Fuchs ◽  
Hans Eklund
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Glutamic Acid ◽  
Structure Analysis ◽  
Crystal Structure Analysis

scholarly journals Complexes between Nucleotide Base and Amino Acid. II. Crystal Structure of 5-Bromocytosine :N-Tosyl-L-glutamic Acid

1976 ◽  
Vol 49 (12) ◽  
pp. 3493-3497 ◽  
Author(s):  
Minoru Ohki ◽  
Akio Takenaka ◽  
Hirotaka Shimanouchi ◽  
Yoshio Sasada
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Glutamic Acid ◽  
Nucleotide Base

scholarly journals Crystal Structure of Cel44A, a Glycoside Hydrolase Family 44 Endoglucanase from Clostridium thermocellum

2007 ◽  
Vol 282 (49) ◽  
pp. 35703-35711 ◽  
Author(s):  
Yu Kitago ◽  
Shuichi Karita ◽  
Nobuhisa Watanabe ◽  
Masakatsu Kamiya ◽  
Tomoyasu Aizawa ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Glutamic Acid ◽  
Glycoside Hydrolase ◽  
Clostridium Thermocellum ◽  
Structural Features ◽  
Glycoside Hydrolase Family ◽  
Wild Type ◽  
H Nmr ◽  
Hydrolase Family

The crystal structure of Cel44A, which is one of the enzymatic components of the cellulosome of Clostridium thermocellum, was solved at a resolution of 0.96Å. This enzyme belongs to glycoside hydrolase family (GH family) 44. The structure reveals that Cel44A consists of a TIM-like barrel domain and a β-sandwich domain. The wild-type and the E186Q mutant structures complexed with substrates suggest that two glutamic acid residues, Glu186 and Glu359, are the active residues of the enzyme. Biochemical experiments were performed to confirm this idea. The structural features indicate that GH family 44 belongs to clan GH-A and that the reaction catalyzed by Cel44A is retaining type hydrolysis. The stereochemical course of hydrolysis was confirmed by a 1H NMR experiment using the reduced cellooligosaccharide as a substrate.

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