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Article

Catalytic and inhibitor-binding properties of some active-site mutants of human carbonic anhydrase I.

European journal of biochemistry - 1 May 1995

Engstrand C, Jonsson B H, Lindskog S

Abstract excerpt

Three isozyme-specific residues in the active site of human carbonic anhydrase I, Val62, His67, and His200, have been changed by site-directed mutagenesis to their counterparts in human carbonic anhydrase II, Asn62, Asn67, and Thr200. A double mutant, containing Asn62 and Asn67, and a triple mutant, containing all three alterations, were also produced. The rates of CO2 hydration and ester hydrolysis catalyzed by...

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Source

Identifiers

PMID: 7758465
DOI: 10.1111/j.1432-1033.1995.tb20516.x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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