Difference between revisions of "YML035C"
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| − | '''Description of YML035C:''' AMP deaminase, tetrameric enzyme that catalyzes the deamination of AMP to form IMP and ammonia; may be involved in regulation of intracellular adenine nucleotide pools<ref name=' | + | '''Description of YML035C:''' AMP deaminase, tetrameric enzyme that catalyzes the deamination of AMP to form IMP and ammonia; may be involved in regulation of intracellular adenine nucleotide pools<ref name='S000061600'>Merkler DJ and Schramm VL (1990) Catalytic and regulatory site composition of yeast AMP deaminase by comparative binding and rate studies. Resolution of the cooperative mechanism. J Biol Chem 265(8):4420-6 {{SGDpaper|S000061600}} PMID 2407736</ref><ref name='S000061601'>Merkler DJ, et al. (1989) AMP deaminase from yeast. Role in AMP degradation, large scale purification, and properties of the native and proteolyzed enzyme. J Biol Chem 264(35):21422-30 |
| − | {{SGDpaper| | + | {{SGDpaper|S000061601}} PMID 2687280</ref> |
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Revision as of 13:05, 31 March 2009
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| Systematic name | YML035C |
| Gene name | AMD1 |
| Aliases | AMD3 |
| Feature type | ORF, Verified |
| Coordinates | Chr XIII:208860..206428 |
| Primary SGDID | S000004498 |
Description of YML035C: AMP deaminase, tetrameric enzyme that catalyzes the deamination of AMP to form IMP and ammonia; may be involved in regulation of intracellular adenine nucleotide pools[1][2]
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Contents
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References
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- ↑ Merkler DJ and Schramm VL (1990) Catalytic and regulatory site composition of yeast AMP deaminase by comparative binding and rate studies. Resolution of the cooperative mechanism. J Biol Chem 265(8):4420-6 SGD PMID 2407736
- ↑ Merkler DJ, et al. (1989) AMP deaminase from yeast. Role in AMP degradation, large scale purification, and properties of the native and proteolyzed enzyme. J Biol Chem 264(35):21422-30 SGD PMID 2687280
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