Literature summary for 2.7.12.2 extracted from

Kinoshita, T.; Hashimoto, T.; Sogabe, Y.; Fukada, H.; Matsumoto, T.; Sawa, M.
High-resolution structure discloses the potential for allosteric regulation of mitogen-activated protein kinase kinase 7 (2017), Biochem. Biophys. Res. Commun., 493, 313-317 .

Search for more literature for 2.7.12.2

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
mutant C218S, to 1.3 A resolution. The C-terminal region connecting to the DVD domain fits into the elongated groove in the N-lobe of the adjacent molecule and works as a negative regulator, fixing the open-type auto-inhibition form	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
C147S	90% of wild-type activity	Homo sapiens
C218S	84% of wild-type activity, mutation drastically augments the protein production and crystallographic resolution. C218S crystals grown under microgravity in a space environment yield a 1.3 A resolution structure	Homo sapiens
C218S/C276S	40% of wild-type activity	Homo sapiens
C218S/C276S/C147S	40% of wild-type activity	Homo sapiens
C218S/C276S/C147S/C296S	20% of wild-type activity	Homo sapiens
C276S	98% of wild-type activity, mutation maintains the specific activity and increases the protein yield	Homo sapiens
C296S	79% of wild-type activity, mutation maintains the specific activity and increases the protein yield	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O14733	-	-

Synonyms

Synonyms	Comment	Organism
MAP2K7	-	Homo sapiens

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
40.8	-	melting temperature, wild-type	Homo sapiens
41.4	-	melting temperature, mutant C218S	Homo sapiens

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Release 2023.1 (January 2023)