scholarly journals Anchimeric-Assisted Spontaneous Hydrolysis of Cyanohydrins Under Ambient Conditions: Implications for Cyanide-Initiated Selective Transformations

2017 ◽  
Vol 23 (36) ◽  
pp. 8756-8765 ◽  
Author(s):  
Jayasudhan Reddy Yerabolu ◽  
Charles L Liotta ◽  
Ramanarayanan Krishnamurthy
Keyword(s):  
Ambient Conditions ◽  
Spontaneous Hydrolysis ◽  
Hydrolysis Of

Highly efficient hydrolysis of ammonia borane by anion (−OH, F−, Cl−)-tuned interactions between reactant molecules and CoP nanoparticles

2017 ◽  
Vol 53 (4) ◽  
pp. 705-708 ◽  
Author(s):  
Zi-Cheng Fu ◽  
Yong Xu ◽  
Sharon Lai-Fung Chan ◽  
Wei-Wei Wang ◽  
Fang Li ◽  
...  
Keyword(s):  
High Performance ◽  
Ammonia Borane ◽  
Ambient Conditions ◽  
Highly Efficient ◽  
Performance System ◽  
Hydrolysis Of ◽  
Nanoparticle Catalyst

An anion-assisted hydrolytic H2-releasing ultra-high performance system involving ammonia borane and a CoP nanoparticle catalyst has been established under ambient conditions.

THE ACETYLATION OF THROMBIN

1959 ◽  
Vol 37 (1) ◽  
pp. 1361-1366 ◽  
Author(s):  
Ricardo H. Landaburu ◽  
Walter H. Seegers
Keyword(s):  
Methyl Ester ◽  
Proteolytic Activity ◽  
Basic Structure ◽  
Amino Groups ◽  
Spontaneous Hydrolysis ◽  
Optimum Ph ◽  
Hydrolysis Of

Purified thrombin-C loses its clotting power upon acetylation. The thrombin-E which is produced during the acetylation has approximately twice the proteolytic activity as the original thrombin-C. Evidently amino groups are not necessary to have thrombin-E activity, but if o-acyl groups are also produced the enzyme does not hydrolyze p-toluenesulphonylarginine methyl ester (TAMe). The activity can be recovered by spontaneous hydrolysis of the o-acyl groups at pH 8.5. Thrombin-E does not activate fibrinogen, but does lyse fibrin. The optimum pH with TAMe as substrate is 8.8. It may be that thrombin-C is a dimer of the basic structure in thrombin-E.

Spontaneous Hydrolysis of Glycosides

1998 ◽  
Vol 120 (27) ◽  
pp. 6814-6815 ◽  
Author(s):  
Richard Wolfenden ◽  
Xiangdong Lu ◽  
Gregory Young
Keyword(s):  
Spontaneous Hydrolysis ◽  
Hydrolysis Of

scholarly journals Common-type acylphosphatase: steady-state kinetics and leaving-group dependence

1997 ◽  
Vol 327 (1) ◽  
pp. 177-184 ◽  
Author(s):  
Paolo PAOLI ◽  
Paolo CIRRI ◽  
Lucia CAMICI ◽  
Giampaolo MANAO ◽  
Gianni CAPPUGI ◽  
...  
Keyword(s):  
Inorganic Phosphate ◽  
Strong Dependence ◽  
Common Type ◽  
Enzyme Active Site ◽  
Enzyme Substrate ◽  
Linear Relationships ◽  
Steady State Kinetics ◽  
Spontaneous Hydrolysis ◽  
Leaving Group ◽  
Hydrolysis Of

A number of acyl phosphates differing in the structure of the acyl moiety (as well as in the leaving-group pKa of the acids produced in hydrolysis) have been synthesized. The Km and Vmax values for the bovine common-type acylphosphatase isoenzyme have been measured at 25 °C and pH 5.3. The values of kcat differ widely in relation to the different structures of the tested acyl phosphates: linear relationships between log kcat and the leaving group pKa, as well as between log kcat/Km and the leaving-group pKa, were observed. On the other hand, the Km values of the different substrates are very close to each other, suggesting that the phosphate moiety of the substrate is the main chemical group interacting with the enzyme active site in the formation of the enzyme–substrate Michaelis complex. The enzyme does not catalyse transphosphorylation between substrate and concentrated nucleophilic acceptors (glycerol and methanol); nor does it catalyse H218O–inorganic phosphate oxygen exchange. It seems that no phosphoenzyme intermediate is formed in the catalytic pathway. Furthermore, during the enzymic hydrolysis of benzoyl phosphate in the presence of 18O-labelled water, only inorganic phosphate (and not benzoate) incorporates 18O, suggesting that no acyl enzyme is formed transiently. All these findings, as well as the strong dependence of kcat upon the leaving group pKa, suggest that neither a nucleophilic enzyme group nor general acid catalysis are involved in the catalytic pathway. The enzyme is competitively inhibited by Pi, but it is not inhibited by the carboxylate ions produced during substrate hydrolysis, suggesting that the last step of the catalytic process is the release of Pi. The activation energy values for the catalysed and spontaneous hydrolysis of benzoyl phosphate have been determined.

A Bioinspired Dinickel(II) Hydrolase: Solvent Vapor-Induced Hydrolysis of Carboxyesters under Ambient Conditions

2016 ◽  
Vol 55 (24) ◽  
pp. 12696-12706 ◽  
Author(s):  
Suman K. Barman ◽  
Francesc Lloret ◽  
Rabindranath Mukherjee
Keyword(s):  
Ambient Conditions ◽  
Solvent Vapor ◽  
Hydrolysis Of

Dry ice-mediated rational synthesis of edge-carboxylated crumpled graphene nanosheets for selective and prompt hydrolysis of cellulose and eucalyptus lignocellulose under ambient reaction conditions

2020 ◽  
Vol 22 (16) ◽  
pp. 5437-5446 ◽  
Author(s):  
Hassan Idris Abdu ◽  
Kamel Eid ◽  
Aboubakr M. Abdullah ◽  
Mostafa H. Sliem ◽  
Ahmed Elzatahry ◽  
...  
Keyword(s):  
Graphene Nanosheets ◽  
Ambient Conditions ◽  
Selective Hydrolysis ◽  
Reaction Conditions ◽  
One Pot ◽  
Dry Ice ◽  
Hydrolysis Of Cellulose ◽  
Hydrolysis Of ◽  
Crumpled Graphene

Edge-carboxylated graphene (ECG) crumpled nanosheets with tuneable COOH content were synthesized by a facile one pot approach for selective hydrolysis of cellulose to glucose and eucalyptus to xylose and glucose under ambient conditions.

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