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Literature summary extracted from

  • Douangamath, A.; Walker, M.; Beismann-Driemeyer, S.; Vega-Fernandez, M.C.; Sterner, R.; Wilmanns, M.
    Structural evidence for ammonia tunneling across the (beta alpha)(8) barrel of the imidazole glycerol phosphate synthase bienzyme complex (2002), Structure, 10, 185-193 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.3.2.10 vapor diffusion method Thermotoga maritima

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.3.2.10 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine Thermotoga maritima the enzyme links histidine and de novo purine biosynthesis 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
?
4.3.2.10 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine Thermotoga maritima ATCC 43589 the enzyme links histidine and de novo purine biosynthesis 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.3.2.10 Thermotoga maritima Q9X0C6 AND Q9X0C8 Q9X0C6: subunit HisF, Q9X0C8: subunit HisH
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4.3.2.10 Thermotoga maritima ATCC 43589 Q9X0C6 AND Q9X0C8 Q9X0C6: subunit HisF, Q9X0C8: subunit HisH
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.2.10
-
Thermotoga maritima

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.2.10 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
-
Thermotoga maritima 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
?
4.3.2.10 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine the enzyme links histidine and de novo purine biosynthesis Thermotoga maritima 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
?
4.3.2.10 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
-
Thermotoga maritima ATCC 43589 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
?
4.3.2.10 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine the enzyme links histidine and de novo purine biosynthesis Thermotoga maritima ATCC 43589 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
?

Subunits

EC Number Subunits Comment Organism
4.3.2.10 heterodimer the structure of the enzyme provides a model how ammonia is channeled over a distance of about 25 A. The larger part of the putative ammonia tunnel is provided by the interior of the beta barrel of subunit HisF, which has a (betaalpha)8 fold Thermotoga maritima

Synonyms

EC Number Synonyms Comment Organism
4.3.2.10 ImGP synthase
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Thermotoga maritima

General Information

EC Number General Information Comment Organism
4.3.2.10 metabolism the enzyme links histidine and de novo purine biosynthesis Thermotoga maritima