✦ LIBER ✦

Modular evolution of the purine biosynthetic pathway

✍ Scribed by T Joseph Kappock; Steven E Ealick; JoAnne Stubbe

Book ID: 104414466
Publisher: Elsevier Science
Year: 2000
Tongue: English
Weight: 429 KB
Volume: 4
Category: Article
ISSN: 1367-5931
DOI: 10.1016/s1367-5931(00)00133-2

No coin nor oath required. For personal study only.

✦ Synopsis

Structural studies, sequence alignments, and biochemistry have provided new insights into the evolution of the purine biosynthetic pathway. The importance of chemistry, the binding of ribose 5-phosphate (common to all purine biosynthetic intermediates), and transient protein-protein interactions in channeling of chemically unstable intermediates have all been examined in the past few years.

📜 SIMILAR VOLUMES

Structural and functional modularity of

Structural and functional modularity of proteins in the de novo purine biosynthetic pathway

✍ Hui Li; Walter Fast; Stephen J. Benkovic 📂 Article 📅 2009 🏛 Cold Spring Harbor Laboratory Press 🌐 English ⚖ 655 KB

## Abstract It is generally accepted that naturally existing functional domains can serve as building blocks for complex protein structures, and that novel functions can arise from assembly of different combinations of these functional domains. To inform our understanding of protein evolution and e

Early evolution of the histidine biosynt

Early evolution of the histidine biosynthetic pathway

✍ Renato Fani; Elena Mori; Antonio Lazcano 📂 Article 📅 1996 🏛 Springer Netherlands 🌐 English ⚖ 120 KB

Synthesis of 32P-labeled intermediates o

Synthesis of 32P-labeled intermediates on the purine biosynthetic pathway

✍ Ryan A. Mehl; Tadhg P. Begley 📂 Article 📅 2002 🏛 John Wiley and Sons 🌐 French ⚖ 79 KB 👁 1 views

## Abstract A fast and efficient route to ^32^P‐labeled intermediates on the purine biosynthetic pathway is described. Adenosine kinase catalyzes the phosphorylation of 5‐aminoimidazole‐4‐carboxamide ribonucleoside (AICARs) to give [^32^P]‐5‐aminoimidazole‐4‐carboxamide ribonucleotide (AICAR). This

Gene-enzyme relationships of the purine

Gene-enzyme relationships of the purine biosynthetic pathway in Bacillus subtilis

✍ Saxild, Hans Henrik ;Nygaard, Per 📂 Article 📅 1988 🏛 Springer 🌐 English ⚖ 730 KB

The gene-enzyme relationship has been established for most of the steps of the purine de novo biosynthetic pathway in Bacillus subtilis. The synthesis of inosine monophosphate (IMP) involves ten steps, and the branching from IMP to AMP and to guanosine monophosphate (GMP) synthesis both require two

Sequence of the bifunctionalade1gene in

Sequence of the bifunctionalade1gene in the purine biosynthetic pathway of the fission yeastSchizosaccharomyces pombe

✍ Rod McKenzie; Peter Schuchert; Brian Kilbey 📂 Article 📅 1987 🏛 Springer-Verlag 🌐 English ⚖ 681 KB

The adel gene of the fission yeast Schizosaccharomyces pombe encodes a bifunctional polypeptide with glycinamide ribotide synthetase (GARSase) and aminoimidazole ribotide synthetase (AIRSase) enzeyme activities. These enzyme activities carry out the 2nd and 5th steps, respectively, of the purine syn

Multifunctional enzymes and evolution of

Multifunctional enzymes and evolution of biosynthetic pathways: Retro-evolution by jumps

✍ Siddhartha Roy 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 244 KB 👁 1 views

A likely scenario of evolution of biosynthetic pathways is believed to have occurred by retro-evolution through recruitment of existing enzymes rather than generation of de novo classes. It had been proposed that such retro-evolution occurred in steps as a response to depletion of an essential metab