The Carbonic Anhydrases 1991
DOI: 10.1007/978-1-4899-0750-9_2
|View full text |Cite
|
Sign up to set email alerts
|

Structure and Evolutionary Origins of the Carbonic Anhydrase Multigene Family

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

1
10
0

Year Published

1993
1993
2004
2004

Publication Types

Select...
7
2

Relationship

1
8

Authors

Journals

citations
Cited by 36 publications
(11 citation statements)
references
References 84 publications
1
10
0
Order By: Relevance
“…In BCAIII, an additional Trp (W47) is found, leading to a total of eight Trp residues in this isoenzyme. In this position, Ile and Leu are present in HCAI and 11, respectively (Anderson et al, 1972;Henderson et al, 1976;Hewett-Emmet & Tashian, 1991).…”
Section: Structural Descriptionmentioning
confidence: 99%
See 1 more Smart Citation
“…In BCAIII, an additional Trp (W47) is found, leading to a total of eight Trp residues in this isoenzyme. In this position, Ile and Leu are present in HCAI and 11, respectively (Anderson et al, 1972;Henderson et al, 1976;Hewett-Emmet & Tashian, 1991).…”
Section: Structural Descriptionmentioning
confidence: 99%
“…Specifically, isoenzymes I, 11 and III contain six, seven, and eight Trp residues, respectively; the six Trp residues in HCAI are also present in the other two isoenzymes studied, and the seventh Trp in HCAII is conserved in BCAIII (Anderson et al, 1972;Henderson et al, 1976;Hewett-Emmet & Tashian, 1991). Considering the fact that these isoenzymes have almost identical secondary structure, comparisons of their CD spectra should shed some light on the significance of interference by specific Trp residues in the spectrally based prediction of secondary structure content.…”
mentioning
confidence: 99%
“…Carbonic anhydrases (CA; EC 4.2.1.1) are evolutionally old enzymes [Hewett-Emmet and Tashian, 1991]. They are expressed in most tissues of the human body, participating in pH regulation, carbon dioxide and bicarbonate transport, as well as in the maintenance of water and electrolyte balance [Maren, 1967;Tashian, 1989Tashian, , 1992.…”
Section: Introductionmentioning
confidence: 99%
“…Human carbonic anhydrase I (HCA I), also present in red blood cells, is less efficient with a maximal CO, hydration turnover number of about 2X105 s-'. Both isozymes are considered to share the same catalytic mechanism, usually referred to as the zinc-hydroxide mechanism (Ren and Lindskog, 1992 ;Silverman and Lindskog, 1988), described in a simplified version by Eqn (1) and Eqn (2): E-ZnZf-OH-+ CO, -E-ZnZ'-HCO; -E-ZnZ+-HzO + HCO,, The overall three-dimensional structures of the two isozymes are very similar as shown by X-ray crystallography (H%ansson et al, 1992;Kannan et al, 1975), and the amino acid sequences are 60% identical (Hewett-Emmett and Tashian, 1991 ;Tashian, 1989). However, there are some isozyme-specific active site residues that might be associated with the functional differences between HCA I and HCA 11.…”
mentioning
confidence: 87%