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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) [Brown90 ]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic


Enzymatic reaction of: pyrazole synthase

2-pyrazoline + an unknown oxidized electron acceptor <=> pyrazole + an unknown reduced electron acceptor

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 [Brown90]

Inhibitors (Unknown Mechanism): Ca2+ [Brown90]

pH(opt): 6.2 [Brown90]


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

pyrazolidine + an unknown oxidized electron acceptor <=> 2-pyrazoline + an unknown reduced electron acceptor

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 [Brown90]

Inhibitors (Unknown Mechanism): Ca2+ [Brown90]

pH(opt): 6.2 [Brown90]


Enzymatic reaction of: pyrazolidine synthase (pyrazole synthase)

propane-1,3-diamine + an unknown oxidized electron acceptor <=> pyrazolidine + an unknown reduced electron acceptor + 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 [Brown90]

Inhibitors (Unknown Mechanism): Ca2+ [Brown90]

pH(opt): 6.2 [Brown90]


References

Brown90: 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 19.0 on Sat Apr 25, 2015, BIOCYC14A.