Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

MetaCyc Enzyme: pyrazole synthase

Species: Cucumis sativus

Summary:
This partially purified enzyme was demonstrated to convert 1,3-diaminopropane to pyrazole via 2-pyrazoline and thus catalyzes both cyclization of 1,3-diaminopropane and subsequent dehydrogenation to yield pyrazole.

Molecular Weight of Polypeptide: 66 kD (experimental) [Brown90a ]

Gene-Reaction Schematic: ?


Enzymatic reaction of: pyrazole synthase

2-pyrazoline <=> pyrazole + 2 H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

In Pathways: β-pyrazole-1-ylalanine biosynthesis

Summary:
Purification procedure of the cucumber enzyme showed a major activity peak of 66 kDa and a minor peak of 12.6 kDa. The minor peak was speculated of being a peptide fragment during the purification which retained the catalytic activity domain. The enzyme activity was not affected by EDTA and many metal ions, except that Ca2+ is significantly inhibitory. The enzyme has a narrow optimum pH of 6.2. Very little activity can be detected above pH 6.5.

Activators (Unknown Mechanism): FAD [Brown90a]

Inhibitors (Unknown Mechanism): Ca2+ [Brown90a]

pH(opt): 6.2 [Brown90a]


Enzymatic reaction of: 2-pyrazoline synthase (pyrazole synthase)

pyrazolidine <=> 2-pyrazoline + 2 H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

In Pathways: β-pyrazole-1-ylalanine biosynthesis

Summary:
Purification procedure of the cucumber enzyme showed a major activity peak of 66 kDa and a minor peak of 12.6 kDa. The minor peak was speculated of being a peptide fragment during the purification which retained the catalytic activity domain. The enzyme activity was not affected by EDTA and many metal ions, except that Ca2+ is significantly inhibitory. The enzyme has a narrow optimum pH of 6.2. Very little activity can be detected above pH 6.5.

Activators (Unknown Mechanism): FAD [Brown90a]

Inhibitors (Unknown Mechanism): Ca2+ [Brown90a]

pH(opt): 6.2 [Brown90a]


Enzymatic reaction of: pyrazolidine synthase (pyrazole synthase)

propane-1,3-diamine <=> pyrazolidine + 4 H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

In Pathways: β-pyrazole-1-ylalanine biosynthesis

Summary:
Purification procedure of the cucumber enzyme showed a major activity peak of 66 kDa and a minor peak of 12.6 kDa. The minor peak was speculated of being a peptide fragment during the purification which retained the catalytic activity domain. The enzyme activity was not affected by EDTA and many metal ions, except that Ca2+ is significantly inhibitory. The enzyme has a narrow optimum pH of 6.2. Very little activity can be detected above pH 6.5.

Activators (Unknown Mechanism): FAD [Brown90a]

Inhibitors (Unknown Mechanism): Ca2+ [Brown90a]

pH(opt): 6.2 [Brown90a]


References

Brown90a: Brown, E.G., Diffin, F.M. (1990). "Biosynthesis and metabolism of pyrazole by Cucumis sativus: enzymic cyclization and dehydrogenation of 1,3-diaminopropane." Phytochemistry, 1990, 29(2):469-478.


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sat Nov 22, 2014, BIOCYC13B.