Salt dependence, kinetic properties and catalytic mechanism of N-formylmethanofuran:tetrahydromethanopterin formyltransferase from the extreme thermophile Methanopyrus kandleri.

Breitung, J; Börner, G; Scholz, S; Linder, D; Stetter, K O; Thauer, R K

Breitung, J; Börner, G; Scholz, S; Linder, D; Stetter, K O; Thauer, R K.

Affiliation

Breitung J; Laboratorium für Mikrobiologie des Fachbereichs Biologie, Philipps-Universität, Marburg, Federal Republic of Germany.

Eur J Biochem ; 210(3): 971-81, 1992 Dec 15.

Article in En | MEDLINE | ID: mdl-1483480

Subject(s)

Euryarchaeota/enzymology; Hydroxymethyl and Formyl Transferases; Salts/pharmacology; Transferases/metabolism; Amino Acid Sequence; Enzyme Activation; Enzyme Stability; Hot Temperature; Kinetics; Molecular Sequence Data; Sequence Homology, Amino Acid; Species Specificity; Thermodynamics; Transferases/chemistry; Transferases/isolation & purification

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Collection: 01-internacional Database: MEDLINE Main subject: Salts / Transferases / Euryarchaeota / Hydroxymethyl and Formyl Transferases Language: En Journal: Eur J Biochem Year: 1992 Type: Article

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