Role of a disulfide cross-link in the conformational stability of a thermostable xylanase

1990 ◽  
Vol 9 (5) ◽  
pp. 641-646 ◽  
Author(s):  
Utpal Tatu ◽  
S. K. Murthy ◽  
P. J. Vithayathil
Keyword(s):  
Conformational Stability ◽  
Thermostable Xylanase ◽  
Cross Link

Role of surface residues in conformational stability of human lysozyme

2000 ◽  
Vol 28 (5) ◽  
pp. A410-A410
Author(s):  
J. Funahashi ◽  
K. Takano ◽  
Y. Yamagata ◽  
M. Nakasako ◽  
K. Yutani
Keyword(s):  
Conformational Stability ◽  
Human Lysozyme

Role of the internal cross-link in oxytocin. Preparation of mercury mercaptide oxytocin derivatives

Biochemistry ◽  
1974 ◽  
Vol 13 (11) ◽  
pp. 2347-2353 ◽  
Author(s):  
Ruth Sperling ◽  
Marian Gorecki
Keyword(s):  
Cross Link

Role of the FAD-dependent polyamine oxidase in the selective formation of N1,N8-bis(γ- glutamyl)spermidine protein cross-links1

2007 ◽  
Vol 35 (2) ◽  
pp. 396-400 ◽  
Author(s):  
A. Lentini ◽  
P. Mattioli ◽  
B. Provenzano ◽  
A. Abbruzzese ◽  
M. Caraglia ◽  
...  
Keyword(s):  
Stratum Corneum ◽  
Polyamine Oxidase ◽  
Polyamine Metabolism ◽  
Suitable Model ◽  
Cross Link ◽  
Cellular Mechanisms ◽  
Preferential Formation ◽  
Cross Links ◽  
Selective Formation

Protein-bound γ-glutamylpolyamines have highlighted a new pathway in polyamine metabolism. Human foreskin keratinocytes offer a suitable model for this study. Indeed, they develop polymerized envelopes, as they differentiate, rich in ϵ-(γ-glutamyl)lysine and N1,N8-bis(γ-glutamyl)spermidine cross-links. We have found that the selective oxidation of N1-(γ-glutamyl)spermidine and N-(γ-glutamyl)spermine by FAD-dependent polyamine oxidase (PAO) may be one of the cellular mechanisms regulating the preferential formation of a sterically defined bis(γ-glutamyl)spermidine cross-link. The significance of this finding is unknown, but it suggests that the target of this PAO-modulation is to achieve the biochemical prerequisite for production of a normal epidermal stratum corneum.

scholarly journals THE ROLE OF POTASSIUM AND CALSIUM IN IMPROVING THE QUALITY AND SHELF LIFE OF TOMATO (Lycopersicum esculentum var. servo)

el–Hayah ◽  
2019 ◽  
Vol 7 (2) ◽  
pp. 84-93
Author(s):  
Puguh Catur Wicaksana ◽  
Ketut Anom Wijaya ◽  
Sigit Soeparjono
Keyword(s):  
Cell Wall ◽  
Shelf Life ◽  
Cell Wall Regeneration ◽  
Cross Link ◽  
Tomato Production ◽  
High Productivity ◽  
Long Duration ◽  
High Respiration Rate ◽  
Quality And Shelf Life

Tomato has the characteristics natural to damage. Damage fruits are caused by destitute of fruit quality and sensory attributes. The loss of tomato production on harvest in developing countries reached 50% due to the long duration of tomato distribution. Servo varieties of tomatoes are in demand by farmers because of their genetic advantages, high productivity, and abundant fruit weights. The shortage of servo varieties of tomatoes is the short shelf life of fruit, which is seven days after harvest. Short shelf life is influenced by fruit thickness and fruit hardness. In improving the quality and shelf life of tomatoes, potassium (K) nutrition plays a role in photosynthetic translocation, strengthens the cell wall, and involved in the lignification process of sclerenchyma tissue. Tomatoes, as climacteric fruits have a high respiration rate influenced by ethylene. Ethylene production can be inhibited by calcium chloride (CaCl2) application by strengthening the cell wall mechanism, cross-link with pectin, and increase the cell wall regeneration can change the texture of the fruit become harder, and it reduces sensitivity to physiological damage. Based on the treatment of this research, the quality and shelf life of servo varieties of tomato is increased.

scholarly journals The role of an evolutionarily conserved cis-proline in the thioredoxin-like domain of human class Alpha glutathione transferase A1-1

2003 ◽  
Vol 372 (1) ◽  
pp. 241-246 ◽  
Author(s):  
Chris NATHANIEL ◽  
Louise A. WALLACE ◽  
Jonathan BURKE ◽  
Heini W. DIRR
Keyword(s):  
Glutathione Transferase ◽  
Conformational Stability ◽  
Wild Type ◽  
Catalytic Function ◽  
Evolutionarily Conserved ◽  
Glutathione S Transferases ◽  
Equilibrium Unfolding ◽  
The Stability ◽  
Unfolding Kinetics

The thioredoxin-like fold has a βαβαββα topology, and most proteins/domains with this fold have a topologically conserved cis-proline residue at the N-terminus of β-strand 3. This residue plays an important role in the catalytic function and stability of thioredoxin-like proteins, but is reported not to contribute towards the stability of glutathione S-transferases (GSTs) [Allocati, Casalone, Masulli, Caccarelli, Carletti, Parker and Di Ilio (1999) FEBS Lett. 445, 347–350]. In order to further address the role of the cis-proline in the structure, function and stability of GSTs, cis-Pro-56 in human GST (hGST) A1-1 was replaced with a glycine, and the properties of the P56G mutant were compared with those of the wild-type protein. Not only was the catalytic function of the mutant dramatically reduced, so was its conformational stability, as indicated by equilibrium unfolding and unfolding kinetics experiments with urea as denaturant. These findings are discussed in the context of other thioredoxin-like proteins.

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