Deaminase, Myoadenylate
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  Deaminase, Myoadenylate



Deaminase, Myoadenylate

   An enzyme that catalyzes the deamination of AMP to IMP. EC 3.5.4.6.

RELATED TERMS
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Enzyme
A cellular protein whose shape allows it to hold together several other molecules in close proximity to each other. In this way, enzymes are able to induce chemical reactions in other substances with little expenditure of energy and without being changed themselves. Basically, an enzyme acts as a catalyst.

Deamination
The removal of an amino group (NH2) from a chemical compound.



SIMILAR TERMS
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Deamidase, Nicotinamide
An enzyme that catalyzes the hydrolysis of nicotinamide to nicotinate and ammonia. EC 3.5.1.19.

Deaminase, Adenosine
An enzyme that catalyzes the hydrolysis of adenosine to inosine with the elimination of ammonia. Since there are wide tissue and species variations in the enzyme, it has been used as a tool in the study of human and animal genetics and in medical diagnosis. EC 3.5.4.4.

Deaminase, Adenylate
An enzyme that catalyzes the deamination of AMP to IMP. EC 3.5.4.6.

Deaminase, AMP
An enzyme that catalyzes the deamination of AMP to IMP. EC 3.5.4.6.

Deaminase, Asparagine
A hydrolase enzyme that converts L-asparagine and water to L-aspartate and NH3. EC 3.5.1.1.

Deaminase, Cytidine
An enzyme that catalyzes the deamination of cytidine, forming uridine. EC 3.5.4.5.

Deaminase, DCMP
An enzyme that catalyzes the hydrolytic deamination of deoxycytidylic acid to deoxyuridylic acid and ammonia. It plays an important role in the regulation of the pool of deoxynucleotides in higher organisms. The enzyme also acts on some 5-substituted deoxycytidylic acids. EC 3.5.4.12.

Deaminase, Deoxycytidine Monophosphate
An enzyme that catalyzes the hydrolytic deamination of deoxycytidylic acid to deoxyuridylic acid and ammonia. It plays an important role in the regulation of the pool of deoxynucleotides in higher organisms. The enzyme also acts on some 5-substituted deoxycytidylic acids. EC 3.5.4.12.

Deaminase, Deoxycytidylate
An enzyme that catalyzes the hydrolytic deamination of deoxycytidylic acid to deoxyuridylic acid and ammonia. It plays an important role in the regulation of the pool of deoxynucleotides in higher organisms. The enzyme also acts on some 5-substituted deoxycytidylic acids. EC 3.5.4.12.

Deaminase, Ethanolamine
An enzyme that catalyzes the deamination of ethanolamine to acetaldehyde. EC 4.3.1.7.

Deaminase, Guanine
An enzyme that catalyzes the deamination of guanine to form xanthine. EC 3.5.4.3.

Deaminase, Histidine
An enzyme that catalyzes the first step of histidine catabolism, forming UROCANIC ACID and AMMONIA from HISTIDINE. Deficiency of this enzyme is associated with elevated levels of serum histidine. EC 4.3.1.3.

Deaminase, Homoserine
A multifunctional pyridoxal phosphate enzyme. In the final step in the biosynthesis of cysteine it catalyzes the cleavage of cystathionine to yield cysteine, ammonia, and 2-ketobutyrate. EC 4.4.1.1.

Deaminase, Porphobilinogen
An enzyme that catalyzes the formation of hydroxymethylbilane from four molecules of porphobilinogen. EC 4.3.1.8.

Deaminase, Serine
An enzyme of the lyase class that catalyzes the dehydration and deamination of L-serine to form pyruvate. (Dorland, 28th ed) EC 4.2.1.13.

Deaminase, Threonine
A pyridoxal-phosphate protein that catalyzes the deamination of threonine to 2-ketobutyrate and ammonia. The role of this enzyme can be biosynthetic or biodegradative. In the former role it supplies 2-ketobutyrate required for isoleucine biosynthesis, while in the latter it is only involved in the breakdown of threonine to supply energy. EC 4.2.1.16.

Deaminases, Nucleoside
Catalyze the hydrolysis of nucleosides with the elimination of ammonia.

Deaminases, Nucleotide
Catalyze the hydrolysis of nucleotides with the elimination of ammonia.

Deamination
The removal of an amino group (NH2) from a chemical compound.

Deaminations
The removal of an amino group (NH2) from a chemical compound.

Deamino Arginine Vasopressin
A synthetic analog of the pituitary hormone, ARGIPRESSIN. Its action is mediated by the vasopressin receptor V2. It has prolonged antidiuretic activity, but little pressor effects. It also modulates levels of circulating FACTOR VIII and VON WILLEBRAND FACTOR.



PREVIOUS AND NEXT TERMS
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Deaminases, Nucleotide
Catalyze the hydrolysis of nucleotides with the elimination of ammonia.

Deaminases, Nucleoside
Catalyze the hydrolysis of nucleosides with the elimination of ammonia.

Deaminase, Threonine
A pyridoxal-phosphate protein that catalyzes the deamination of threonine to 2-ketobutyrate and ammonia. The role of this enzyme can be biosynthetic or biodegradative. In the former role it supplies 2-ketobutyrate required for isoleucine biosynthesis, while in the latter it is only involved in the breakdown of threonine to supply energy. EC 4.2.1.16.

Deaminase, Serine
An enzyme of the lyase class that catalyzes the dehydration and deamination of L-serine to form pyruvate. (Dorland, 28th ed) EC 4.2.1.13.

Deaminase, Porphobilinogen
An enzyme that catalyzes the formation of hydroxymethylbilane from four molecules of porphobilinogen. EC 4.3.1.8.

Deaminase, Myoadenylate

Death, Cardiac Sudden
Sudden death (DEATH, SUDDEN) that is due to HEART ARREST.

Death, Cardiac
Irreversible cessation of all bodily functions, manifested by absence of spontaneous breathing and total loss of cardiovascular and cerebral functions.

Death, Attitude to
Conceptual response of the person to the various aspects of death, which are based on individual psychosocial and cultural experience.

Death, Attitudes to
Conceptual response of the person to the various aspects of death, which are based on individual psychosocial and cultural experience.

Death, Brain
A state of prolonged irreversible cessation of all brain activity, including lower brain stem function with the complete absence of voluntary movements, responses to stimuli, brain stem reflexes, and spontaneous respirations. Reversible conditions which mimic this clinical state (e.g., sedative overdose, hypothermia, etc.) are excluded prior to making the determination of brain death. (From Adams et al., Principles of Neurology, 6th ed, pp348-9)

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