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Literature summary extracted from

  • Witek, W.; Sliwiak, J.; Ruszkowski, M.
    Structural and mechanistic insights into the bifunctional HISN2 enzyme catalyzing the second and third steps of histidine biosynthesis in plants (2021), Sci. Rep., 11, 9647.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.4.19 expression in Escherichia coli BL21 Gold Medicago truncatula

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.4.19 vapor diffusion method Medicago truncatula
3.6.1.31
-
 Medicago truncatula

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.4.19 AMP inhibitor of the PRA-CH domain of the enzyme at physiologically-relevant concentrations Medicago truncatula

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.1.31 Mg2+ required Medicago truncatula

Organism

EC Number Organism UniProt Comment Textmining
3.5.4.19 Medicago truncatula A0A072U2X9
-
-
3.6.1.31 Medicago truncatula A0A072U2X9 bifunctional enzyme, two distinct domains are active respectively as a phosphoribosyl-AMP cyclohydrolase (PRA-CH, EC 3.5.4.19) and phosphoribosyl-ATP diphosphatase (PRA-PH, EC 3.6.1.31)
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.4.19 leaf
-
 Medicago truncatula
-

Subunits

EC Number Subunits Comment Organism
3.6.1.31 dimer HISN2 forms a dimeric enzyme with discrete and directly interacting pyrophosphohydrolase and cyclohydrolase domains, crystallization data. The PRA-PH domain consists of two overlapping and swapped protein chains built entirely of alpha-helices connected by loops Medicago truncatula

Synonyms

EC Number Synonyms Comment Organism
3.5.4.19 HisN2 bifunctional enzyme, cf. EC 3.6.1.31 Medicago truncatula
3.6.1.31 HisIE
-
 Medicago truncatula
3.6.1.31 HisN2
-
 Medicago truncatula

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.6.1.31 Medicago truncatula calculated from sequence
-
 5.3

General Information

EC Number General Information Comment Organism
3.5.4.19 evolution the calculated sequence similarity networks between HISN2 analogs from prokaryotes and eukaryotes suggest that the plant enzymes are closest relatives of those in the class of Deltaproteobacteria Medicago truncatula
3.5.4.19 metabolism the bifunctional enzyme (cf. EC 3.6.1.31) catalyzes two steps of the histidine biosynthetic pathway in plants Medicago truncatula
3.6.1.31 additional information in the bifunctional enzyme, phosphoribosyl-AMP intermediate is released between the two catalytic events Medicago truncatula