Primary Information |
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| BoMiProt ID | Bomi321 |
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| Protein Name | Bifunctional purine biosynthesis protein PURH |
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| Organism | Bos taurus |
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| Uniprot ID | Q0VCK0 |
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| Milk Fraction | Whey, MFGM, Exosome |
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| Ref Sequence ID | NP_001068722.1 |
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| Aminoacid Length | 592 |
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| Molecular Weight | 64483 |
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| FASTA Sequence |
Download |
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| Gene Name | ATIC |
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| Gene ID | 506343 |
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| Protein Existence Status | Reviewed: Experimental evidence at transcript level |
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Secondary Information |
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| Protein Function | catalyzes the transfer of a formyl group from the
cofactor N10-formyltetrahydrofolate (10-f-THF) to the substrate
AICAR to produce the stable intermediate 5-formyl-
AICAR (FAICAR) and the byproduct tetrahydrofolate; enzymes in the de novo purine
biosynthetic pathway |
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| Biochemical Properties | 10-f-H2F is an alternative cofactor for human
AICAR Tfase, and since it is more stable than 10-f-H4F and
has a lower Km; formylation of AICAR by 10-f-
H2F is reversible with an equilibrium constant of 0.024 |
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| PTMs | N-acetylation at methionine,Lysine |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Bibliography | 1. Wolan, D. W. et al. (2004) ‘Structural Insights into the Human and Avian IMP Cyclohydrolase Mechanism via Crystal Structures with the Bound XMP Inhibitor † , ‡’, Biochemistry, 43(5), pp. 1171–1183. doi: 10.1021/bi030162i.
2. Wall, M., Shim, J. H. and Benkovic, S. J. (2000) ‘Human AICAR Transformylase: Role of the 4-Carboxamide of AICAR in Binding and Catalysis †’, Biochemistry, 39(37), pp. 11303–11311. doi: 10.1021/bi0007268. |
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