Evolution of Enzymatic Activities in the Orotidine 5‘-Monophosphate Decarboxylase Suprafamily:  Enhancing the Promiscuousd-arabino-Hex-3-ulose 6-Phosphate Synthase Reaction Catalyzed by 3-Keto-l-gulonate 6-Phosphate Decarboxylase†

Biochemistry ◽  
2005 ◽  
Vol 44 (6) ◽  
pp. 1807-1815 ◽  
Author(s):  
Wen Shan Yew ◽  
Julie Akana ◽  
Eric L. Wise ◽  
Ivan Rayment ◽  
John A. Gerlt
Keyword(s):  
Enzymatic Activities ◽  
Monophosphate Decarboxylase ◽  
Phosphate Synthase

Crystal structure of 3-hexulose-6-phosphate synthase, a member of the orotidine 5′-monophosphate decarboxylase suprafamily

2010 ◽  
Vol 78 (16) ◽  
pp. 3488-3492 ◽  
Author(s):  
Izumi Orita ◽  
Akiko Kita ◽  
Hiroya Yurimoto ◽  
Nobuo Kato ◽  
Yasuyoshi Sakai ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Monophosphate Decarboxylase ◽  
Phosphate Synthase

scholarly journals Crystallization of 3-hexulose-6-phosphate synthase

2021 ◽  
Vol 12 (3) ◽  
pp. 299-303
Author(s):  
Masoud Delfi ◽  
Leila Mahdavian ◽  
Mohammad Sattarifar ◽  
Nina Hakulinen ◽  
Juha Rouvinen
Keyword(s):  
Structural Characterization ◽  
Active Site ◽  
Aldol Condensation ◽  
Maximum Activity ◽  
Site Structure ◽  
Monophosphate Decarboxylase ◽  
Key Enzyme ◽  
Ribulose Monophosphate Cycle ◽  
Active Site Structure ◽  
Phosphate Synthase

The crystal structures can reveal detailed information about the overall structure, active site structure, and functional mechanism of enzymes. This study focused on the crystallization of 3-hexulose-6-phosphate synthase from Methylomonas aminofaciens 77a, to produce higher resolution crystals for precise structural characterization. 3-Hexulose-6-phosphate synthase is from Methylomonas aminofaciens 77a (EC 4.1.2.43). It belongs to the orotidine 5'-monophosphate decarboxylase superfamily, and acts as a key enzyme for a ribulose-monophosphate cycle of formaldehyde fixation and detoxification. 3-Hexulose-6-phosphate synthase catalyzes the aldol condensation of formaldehyde with D-ribulose-5-phosphate. For the maximum activity, 3-hexulose-6-phosphate synthase requires Mg2+ or Mn2+ as ligands. MaHPS crystallized at the concentration of 7 mg/mL and conditions consisting of 0.2 M MgCl2, 18% PEG 3350 at pH = 7.0.

GENE-ENZYME RELATIONS OF TRYPTOPHAN MUTANTS IN STREPTOMYCES COELICOLOR A3(2)

Genetics ◽  
1974 ◽  
Vol 78 (3) ◽  
pp. 799-808
Author(s):  
Charles M Smithers ◽  
Paulinus P Engel
Keyword(s):  
Streptomyces Coelicolor ◽  
Enzymatic Activities ◽  
Tryptophan Synthase ◽  
Phosphate Synthase

ABSTRACT Mutations in twenty-eight tryptophan mutants of S. coelicolor A3(2) were mapped relative to the nearest flanking markers. Mutants lacking single enzymatic activities for phosphoribosyltransferase, phosphoribosylanthranilate isomerase, indodeglycerol phosphate synthase, tryptophan synthase A and tryptophan synthase B were identified.

Sensitive Genome-Wide Screen for Low Secondary Enzymatic Activities: The YjbQ Family Shows Thiamin Phosphate Synthase Activity

2008 ◽  
Vol 376 (3) ◽  
pp. 839-853 ◽  
Author(s):  
Enrique Morett ◽  
Gloria Saab-Rincón ◽  
Leticia Olvera ◽  
Maricela Olvera ◽  
Humberto Flores ◽  
...  
Keyword(s):  
Enzymatic Activities ◽  
Genome Wide ◽  
Thiamin Phosphate Synthase ◽  
Phosphate Synthase
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