Edge Rewrite
// HTMLRewriter · presentation

This page was redesigned at the edge.

Cloudflare fetched the original article and streamed it through HTMLRewriter to apply an entirely new visual system without rebuilding the source page.

// request.cf · coarse context

A page that knows where it met you.

Only coarse request metadata is shown. This demo does not display or persist visitor IP addresses.

Country
US
Cloudflare location
CMH
Connection
HTTP/2
Language
Not provided

Ray ID: a2accf765d67cf52

Jump to content

// Workers AI · dad joke modeWhat did 2-methylisocitrate dehydratase say? "I'm dehydrated".

From Wikipedia, the free encyclopedia
2-methylisocitrate dehydratase
Identifiers
EC no.4.2.1.99
CAS no.170780-51-5
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

The enzyme 2-methylisocitrate dehydratase (EC 4.2.1.99) catalyzes the chemical reaction

(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate (Z)-but-2-ene-1,2,3-tricarboxylate + H2O

This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate hydro-lyase [(Z)-but-2-ene-1,2,3-tricarboxylate-forming]. This enzyme is also called (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate hydro-lyase. This enzyme participates in propanoate metabolism.

References

[edit]
  • Aoki H, Uchiyama H, Umetsu H, Tabuchi T (1995). "Isolation of 2-methylisocitrate dehydratase, a new enzyme serving in the methylcitric acid cycle for propionate metabolism, from Yarrowia lipolytica". Biosci. Biotechnol. Biochem. 59 (10): 1825–1828. doi:10.1271/bbb.59.1825.
  • Tabuchi T, Umetsu H, Aoki H, Uchiyama H (1995). "Characteristics of 2-methylisocitrate dehydratase, isolated from Yarrowia lipolytica, in comparison to aconitase". Biosci. Biotechnol. Biochem. 59 (11): 2013–2017. doi:10.1271/bbb.59.2013.