Literature summary for 5.6.2.3 extracted from

Gu, Y.; Masuda, Y.; Kamiya, K.
Biochemical analysis of human PIF1 helicase and functions of its N-terminal domain (2008), Nucleic Acids Res., 36, 6295-6308.

Search for more literature for 5.6.2.3

Activating Compound

Activating Compound	Comment	Organism	Structure
single-stranded DNA	nonstructural single-stranded DNA greatly stimulates ATPase activity due to a high affinity for PIF1, even though PIF1 preferentially unwinds forked substrates. The N-terminal portion oF PIF1 helicase, named the PIF1 N-terminal (PINT) domain, contributes to enhancing the interaction with single-stranded DNA through intrinsic binding activity	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
replication protein A	inhibits unwinding and annealing activities	Homo sapiens

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0038	-	ATP	pH 8.0, 30°C, with saturating concentration of M13 mp18 ssDNA	Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
71000	-	1 * 71000, SDS-PAGE	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9H611	-	-

Purification (Commentary)

Purification (Comment)	Organism
full-length PIF1 with a 6* histidine tag at the N-terminus, a C-terminal truncated form (PIF1N) and a N-terminal truncated form (PIF1C)	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O	-	Homo sapiens	ADP + phosphate	-	?

Subunits

Subunits	Comment	Organism
monomer	1 * 71000, SDS-PAGE	Homo sapiens

Synonyms

Synonyms	Comment	Organism
PIF1	-	Homo sapiens
PIF1 helicase	-	Homo sapiens

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Release 2023.1 (January 2023)