Kinetic and mutational dissection of the two ATPase activities of terminase, the DNA packaging enzyme of bacteriophage Chi.

doi:10.1021/bi952322z

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Article

Kinetic and mutational dissection of the two ATPase activities of terminase, the DNA packaging enzyme of bacteriophage Chi.

Biochemistry - 27 Feb 1996

Hwang Y, Catalano C E, Feiss M

Abstract excerpt

Terminase the DNA packaging enzyme of bacteriophage chi, is a heteromultimer of gpNul (21 kDa) and gpA (74 kDa) subunits, encoded by the chi Nul and A genes, respectively. Sequence comparisons indicate that both gpNu1 and gpA have a match to the P-loop motif of ATPase centers, which is a glycine-...

Topics

Adenosine Triphosphatases
Adenosine Triphosphate
Affinity Labels
Amino Acid Sequence
Azides
Bacteriophage lambda
Endodeoxyribonucleases
Genes, Viral
Kinetics
Molecular Sequence Data
Molecular Weight
Mutagenesis, Site-Directed
Mutation
Protein Conformation

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Identifiers

PMID: 8611586
DOI: 10.1021/bi952322z

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8611586-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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