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Article

Role of an evolutionarily invariant serine for the stability of human carbonic anhydrase II.

Biochimica et biophysica acta - 9 Jan 1992

Mårtensson L G, Jonsson B H, Andersson M, Kihlgren A, Bergenhem N, Carlsson U

Abstract excerpt

There are several evolutionarily invariant amino acids in the primary structures of all known isoenzymes of carbonic anhydrase. One of these is Ser-29 which is situated in the peripheral part of the active site interacting by hydrogen bonds with amino acids located nearby in the tertiary structure. Furthermore, the neighbourhood of Ser-29, composed of Gln-28, Pro-30, Tyr-194, Ser-197 and Trp-209, has a totally...

Topics

Alanine
Binding Sites
Biological Evolution
Carbonic Anhydrases
Cysteine
Erythrocytes
Humans
Mutation
Protein Conformation
Serine

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Identifiers

PMID: 1730037
DOI: 10.1016/0167-4838(92)90148-7

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1730037-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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