Biochemistry at Maastricht University | Flashcards & Summaries

Lernmaterialien für biochemistry an der Maastricht University

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Oxidoreductases
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Catalyse Oxidation reduction reactions which involve electron transfer 
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Transferases
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Catalyse the transfer of functional groups. For example an amino group or phosphate group. 
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Hydrolases
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Catalyse the hydrolytic removal of a group from the substrate, which will transferred to water 
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Lyases
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 Catalyse reactions which involve the addition of functional groups to break double bonds or the removal of functional groups to form double bonds. 
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Isomerases
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Catalyse reactions that transfer functional groups within a molecule so that isomeric forms are produced
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Ligases
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Catalyze the joining of two molecules by creating a new chemical bond. This usually goes along with the hydrolysis of a pyrophosphate group of ATP
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4 basic principles that enzymes use
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Covalent catalysis
Acid base catalysis
Catalysis by approximation 
metal ion catalysis
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Covalent catalysis
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The enzyme covalently binds to the substrate and holds on to the electrons, serving as a electron carrier 
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Acid base catalysis
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The enzyme serves as a proton donor or acceptor 
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Catalysis by approximation
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The enzyme increases the likelihood of successful collisions, by helping the molecules to be in the right orientation. This is based on that for a reaction to occur, the molecules need to be in the right Orientation and there needs to be sufficient energy
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Metal ion catalysis 
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Enzymes use metal atoms as cofactors. Metal atoms have the ability to lose electrons very easily, which gives them a positive charge. The positive charge can be used to interact with different molecules in the active site. This:
- stabilizes the transition state 
- assist in forming a nucleophile 
- holds the substrate in the active site 

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Nucleophile
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Molecule that has a tendency to donate electrons 
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Beispielhafte Karteikarten für deinen biochemistry Kurs an der Maastricht University - von Kommilitonen auf StudySmarter erstellt!

Q:
Oxidoreductases
A:
Catalyse Oxidation reduction reactions which involve electron transfer 
Q:
Transferases
A:
Catalyse the transfer of functional groups. For example an amino group or phosphate group. 
Q:
Hydrolases
A:
Catalyse the hydrolytic removal of a group from the substrate, which will transferred to water 
Q:
Lyases
A:
 Catalyse reactions which involve the addition of functional groups to break double bonds or the removal of functional groups to form double bonds. 
Q:
Isomerases
A:
Catalyse reactions that transfer functional groups within a molecule so that isomeric forms are produced
Mehr Karteikarten anzeigen
Q:
Ligases
A:
Catalyze the joining of two molecules by creating a new chemical bond. This usually goes along with the hydrolysis of a pyrophosphate group of ATP
Q:
4 basic principles that enzymes use
A:
Covalent catalysis
Acid base catalysis
Catalysis by approximation 
metal ion catalysis
Q:
Covalent catalysis
A:
The enzyme covalently binds to the substrate and holds on to the electrons, serving as a electron carrier 
Q:
Acid base catalysis
A:
The enzyme serves as a proton donor or acceptor 
Q:
Catalysis by approximation
A:
The enzyme increases the likelihood of successful collisions, by helping the molecules to be in the right orientation. This is based on that for a reaction to occur, the molecules need to be in the right Orientation and there needs to be sufficient energy
Q:
Metal ion catalysis 
A:
Enzymes use metal atoms as cofactors. Metal atoms have the ability to lose electrons very easily, which gives them a positive charge. The positive charge can be used to interact with different molecules in the active site. This:
- stabilizes the transition state 
- assist in forming a nucleophile 
- holds the substrate in the active site 

Q:
Nucleophile
A:
Molecule that has a tendency to donate electrons 
biochemistry

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