Literature summary for 3.5.4.27 extracted from

Carbone, V.; Schofield, L.R.; Beattie, A.K.; Sutherland-Smith, A.J.; Ronimus, R.S.
The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from Methanobrevibacter ruminantium (2013), Proteins, 81, 2064-2070.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Methanobrevibacter ruminantium

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of apoenzyme is solved at 1.37 A resolution	Methanobrevibacter ruminantium

Organism

Organism	UniProt	Comment	Textmining
Methanobrevibacter ruminantium	D3E4S5	-	-
Methanobrevibacter ruminantium DSM 1093	D3E4S5	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Methanobrevibacter ruminantium

Subunits

Subunits	Comment	Organism
trimer	-	Methanobrevibacter ruminantium

General Information

General Information	Comment	Organism
physiological function	the enzyme is involved in the methanogenesis pathway of archaea as a C1 unit carrier	Methanobrevibacter ruminantium

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Release 2023.1 (January 2023)