[(2R,3S,4R,5R)-5-(1-amino-2-formamidoethylidene)azaniumyl-3,4-dihydroxyoxolan-2-yl]methyl phosphate

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: [(2R,3S,4R,5R)-5-(1-amino-2-formamidoethylidene)azaniumyl-3,4-dihydroxyoxolan-2-yl]methyl phosphate
• 化学式: C8H15N3O8P-
• 分子量: 312.19
• InChiKey: PMCOGCVKOAOZQM-XVFCMESISA-M

计算性质

• 辛醇/水分配系数(LogP)：
  -4.7
• 重原子数：
  20
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.75
• 拓扑面积：
  191
• 氢给体数：
  5
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  [(2R,3S,4R,5R)-5-(1-amino-2-formamidoethylidene)azaniumyl-3,4-dihydroxyoxolan-2-yl]methyl phosphate 、 adenosine 5'-triphosphate 生成 5-amino-1-(5-phosphonato-beta-D-ribosyl)imidazol-3-ium 、 adenosine 5'-diphosphate 、 氢(+1)阳离子 、 H3PO4
  参考文献：
  名称：

  LEVENBERG B.; BUCHANAN J.M., J Biol Chem, 1957, 0021-9258, 1005-18

  摘要：

  DOI：
• 作为产物：
  描述：

  adenosine 5'-triphosphate 、 水 、 L-谷氨酰胺 、 5'-phosphoribosyl-N-formylglycineamide 生成 [(2R,3S,4R,5R)-5-(1-amino-2-formamidoethylidene)azaniumyl-3,4-dihydroxyoxolan-2-yl]methyl phosphate 、 adenosine 5'-diphosphate 、 氢(+1)阳离子 、 2-氨基戊二酸酯 、 H3PO4
  参考文献：
  名称：

  来自大肠杆菌的甲酰甘氨酰胺核糖核苷酸合成酶：克隆，测序，过量生产，分离和表征。

  摘要：

  大肠杆菌的purL基因编码甲酰甘氨酰胺核糖核苷酸（FGAM）合成酶，可催化甲酰甘氨酰胺核糖核苷酸（FGAR），谷氨酰胺和MgATP向FGAM，谷氨酸，ADP和Pi的转化。由结构基因序列推导的成熟蛋白质包含1628个氨基酸，Mr估计为141,418。purL控制区与其他purloci控制区的比较揭示了一个dyad对称的共同区域，它可能是“推定”阻遏蛋白的结合位点。高产菌株的构建允许将蛋白质纯化至均质。N端序列分析和谷氨酰胺结合结构域序列的比较（Ebbole＆Zalkin，1987）证实了从基因序列推导的氨基酸序列。纯化的蛋白质显示的谷氨酰胺酶活性为正常营业额的0.02％，NH3可以替代Km = 1 M和3 min-1营业额（2％的谷氨酰胺营业额）的谷氨酰胺作为氮供体。该酶与谷氨酰胺形成可分离的（1：1）配合物：t1 / 2在4摄氏度下为22分钟。添加FGAR和ATP时，这种分离的配合物在化学

  DOI：

  10.1021/bi00432a017

文献信息

• LEVENBERG B.; BUCHANAN J.M., J Biol Chem, 1957, 0021-9258, 1019-27
  作者：LEVENBERG B.、BUCHANAN J.M.

  DOI：——

  日期：——
• Structural biology of the purine biosynthetic pathway
  作者：Y. Zhang、M. Morar、S. E. Ealick

  DOI：10.1007/s00018-008-8295-8

  日期：2008.12

  Purine biosynthesis requires ten enzymatic transformations to generate inosine monophosphate. PurF, PurD, PurL, PurM, PurC, and PurB are common to all pathways, while PurN or PurT, PurK/PurE-I or PurE-II, PurH or PurP, and PurJ or PurO catalyze the same steps in different organisms. X-ray crystal structures are available for all 15 purine biosynthetic enzymes, including 7 ATP-dependent enzymes, 2 amidotransferases and 2 tetrahydrofolate-dependent enzymes. Here we summarize the structures of the purine biosynthetic enzymes, discuss similarities and differences, and present arguments for pathway evolution. Four of the ATP-dependent enzymes belong to the ATP-grasp superfamily and 2 to the PurM superfamily. The amidotransferases are unrelated, with one utilizing an N-terminal nucleophileglutaminase and the other utilizing a triad glutaminase. Likewise the tetrahydrofolate-dependent enzymes are unrelated. Ancestral proteins may have included a broad specificity enzyme instead of PurD, PurT, PurK, PurC, and PurP, and a separate enzyme instead of PurM and PurL.
• Purification of, Generation of Monoclonal Antibodies to, and Mapping of Phosphoribosyl N-Formylglycinamide Amidotransferase
  作者：Tristan S. Barnes、John H. Bleskan、Iris M. Hart、Katy A. Walton、Jeffrey W. Barton、David Patterson

  DOI：10.1021/bi00173a031

  日期：1994.2.22

  5'-Phosphoribosyl N-formylglycinamide (FGAR) amidotransferase (EC 6.3.5.3) catalyzes the fourth reaction in the de novo synthesis of purines, that is, the conversion of FGAR to 5'-phosphoribosyl N-formylglycinamidine (FGAM). This is the only step of the pathway for which a vertebrate gene has not been cloned. FGAR amidotransferase has been highly purified from Chinese hamster ovary (CHO) cells, and this preparation has been used to generate monoclonal antibodies in mice. Two of these antibodies, designated BD4 and DD2, have been shown to recognize a 150-kDa protein in CHO-K1 cells that is of very low abundance in Ade-B cells, a CHO line in which FGAR amidotransferase activity is undetectable. Furthermore, the protein recognized by these antibodies is 5-10-fold more abundant in Az(r) cells. The CHO Az(r) cell line was made resistant to azaserine, a potent inhibitor of FGAR amidotransferase; and displays a 5-10-fold increase in FGAR amidotransferase activity over the parental K1 line. FGAR amidotransferase activity and the 150-kDa protein recognized by both monoclonal antibodies were found to immunoprecipitate concomitantly using antibody BD4. Monoclonal antibody DD2 cross-reacted with a human protein of identical molecular mass. A number of Ade-B/human hybrid cells were generated by somatic cell fusion and subsequent 5-bromo-2-deoxyuridine segregation. Analysis of these lines, together with two independently generated human/mouse hybrid cell lines, by both cytogenetics and immunoblotting with antibody DD2 revealed that the human FGAR amidotransferase gene is located on chromosome 17p.
• MELNICK I.; BUCHANAN J.M., J Biol Chem, 1957, 0021-9258, 157-62
  作者：MELNICK I.、BUCHANAN J.M.

  DOI：——

  日期：——
• The Formylglycinamide Ribonucleotide Amidotransferase Complex from <i>Bacillus subtilis</i>:  Metabolite-Mediated Complex Formation
  作者：Aaron A. Hoskins、Ruchi Anand、Steven E. Ealick、JoAnne Stubbe

  DOI：10.1021/bi049127h

  日期：2004.8.1

  Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP- and glutamine-dependent formation of formylglycinamidine ribonucleotide, ADP, Pi, and glutamate in the fourth step of de novo purine biosynthesis. Like all amidotransferases (ATs), FGAR-AT is proposed to channel ammonia between a glutaminase and AT domain. In Gram-negative bacteria and eukaryotes, FGAR-AT is a single similar to 140 kDa protein. In archae and Gram-positive bacteria, the FGAR-AT is formed from three proteins: PurS (10 kDa), PurQ (25 kDa, a glutaminase), and smPurL (80 kDa, an AT). This is the only known AT to require a third structural component (PurS) for activity. Here we report the first purification and biochemical characterization of a three-component AT from Bacillus subtilis. Efforts to isolate an intact FGAR-AT focused initially on coexpression of PurS, smPurL, and PurQ. However, all attempts to purify the complex resulted in separation of the constituent proteins. PurS, smPurL, and PurQ were therefore separately expressed and purified to homogeneity. PurQ had a glutaminase activity of 0.002 s(-1), and smPurL had an ammonia-dependent AT activity of 0.044 s(-1). Reconstitution of PurS, smPurL, and PurQ at a ratio of 2:1:1 gave an activity of 2.49 s(-1), similar to that previously reported for the Escherichia coli 140 kDa FGAR-AT (5.00 s(-1)). PurS was essential for the glutamine-dependent FGAR-AT activity. Surprisingly, activity was found to be absolutely dependent on the presence of Mg2+ and ADP, and a stable FGAR-AT complex of 2PurS/1smPurL/1PurQ was detected only in the presence of Mg2+, ADP, and glutamine. The implications of these observations are discussed with respect to ammonia channeling.