Catalytic Properties of Murine Carbonic Anhydrase IV

Hurt, Jonathan D.; Tu, Cong; Laipis, Philip J.; Silverman, David N.

doi:10.1074/jbc.272.21.13512

Cited by 40 publications

(37 citation statements)

References 39 publications

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“…We suggest that the SKIE for the reductive dehalogenase from D. chlororespirans might originate from the rate-limiting deprotonation of a water molecule, because deuterium from solvent is incorporated specifically into the carbon of 2,5-dichlorobenzoate that undergoes dehalogenation by cell extracts of D. tiedjei (44). A similar situation occurs in carbonic anhydrase, where 2 H 2 O SKIEs between 2 and 3.8 are observed (36,(45)(46)(47)(48). The SKIE studies seem most consistent with path B of Fig.…”

Section: Kinetic Properties Of the D Chlororespirans Dehalogenase-insupporting

confidence: 73%

Characterization of the B12- and Iron-Sulfur-containing Reductive Dehalogenase fromDesulfitobacterium chlororespirans

Krasotkina

Walters

Maruya

et al. 2001

Journal of Biological Chemistry

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The United Nations and the U.S. Environmental Protection Agency have identified a variety of chlorinated aromatics that constitute a significant health and environmental risk as "priority organic pollutants," the socalled "dirty dozen." Microbes have evolved the ability to utilize chlorinated aromatics as terminal electron acceptors in an energy-generating process called dehalorespiration. In this process, a reductive dehalogenase (CprA), couples the oxidation of an electron donor to the reductive elimination of chloride. We have characterized the B 12 and iron-sulfur cluster-containing 3-chloro-4-hydroxybenzoate reductive dehalogenase from Desulfitobacterium chlororespirans. By defining the substrate and inhibitor specificity for the dehalogenase, the enzyme was found to require an hydroxyl group ortho to the halide. Inhibition studies indicate that the hydroxyl group is required for substrate binding. The carboxyl group can be replaced by other functionalities, e.g. acetyl or halide groups, ortho or meta to the chloride to be eliminated. The purified D. chlororespirans enzyme could dechlorinate an hydroxylated PCB (3,3,5,5-tetrachloro-4,4-biphenyldiol) at a rate about 1% of that with 3-chloro-4-hydroxybenzoate. Solvent deuterium isotope effect studies indicate that transfer of a single proton is partially rate-limiting in the dehalogenation reaction.

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Section: Kinetic Properties Of the D Chlororespirans Dehalogenase-insupporting

confidence: 73%

Characterization of the B12- and Iron-Sulfur-containing Reductive Dehalogenase fromDesulfitobacterium chlororespirans

Krasotkina

Walters

Maruya

et al. 2001

Journal of Biological Chemistry

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“…Similar isotope effects on k cat were reported for the bovine CA III ␣-class carbonic anhydrase (45), the ␥-class enzyme Cam (1), and the P. sativum ␤-class carbonic anhydrase (30). The observed solvent hydrogen isotope effect on k cat of 2.1 for Cab is smaller than the value of 3.8 reported for human ␣-class CA II (55), but similar to the value reported for human ␣-class CA IV (27), which follows a mechanism similar to that of CA II.…”

Section: Discussionsupporting

confidence: 51%

Structural and Kinetic Characterization of an Archaeal β-Class Carbonic Anhydrase

et al. 2000

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The ␤-class carbonic anhydrase from the archaeon Methanobacterium thermoautotrophicum (Cab) was structurally and kinetically characterized. Analytical ultracentrifugation experiments show that Cab is a tetramer. Circular dichroism studies of Cab and the Spinacia oleracea (spinach) ␤-class carbonic anhydrase indicate that the secondary structure of the ␤-class enzymes is predominantly ␣-helical, unlike that of the ␣-or ␥-class enzymes. Extended X-ray absorption fine structure results indicate the active zinc site of Cab is coordinated by two sulfur and two O/N ligands, with the possibility that one of the O/N ligands is derived from histidine and the other from water. Both the steady-state parameters k cat and k cat /K m for CO 2 hydration are pH dependent. The steady-state parameter k cat is buffer-dependent in a saturable manner at both pH 8.5 and 6.5, and the analysis suggested a ping-pong mechanism in which buffer is the second substrate. At saturating buffer conditions and pH 8.5, k cat is 2.1-fold higher in H 2 O than in D 2 O, consistent with an intramolecular proton transfer step being rate contributing. The steady-state parameter k cat /K m is not dependent on buffer, and no solvent hydrogen isotope effect was observed. The results suggest a zinc hydroxide mechanism for Cab. The overall results indicate that prokaryotic ␤-class carbonic anhydrases have fundamental characteristics similar to the eukaryotic ␤-class enzymes and firmly establish that the ␣-, ␤-, and ␥-classes are convergently evolved enzymes that, although structurally distinct, are functionally equivalent.The thermophilic archaeon Methanobacterium thermoautotrophicum obtains energy for growth by the reduction of CO 2 to CH 4 and is also an obligate chemolithoautotroph; thus, this organism has a high demand for CO 2 . Carbonic anhydrase, a zinc-containing enzyme catalyzing the reversible hydration of carbon dioxide (equation 1)is expected to play an important role in the growth of M. thermoautotrophicum and may have several functions, including transporting HCO 3 Ϫ into the cell and providing CO 2 or HCO 3 Ϫ to enzymes that utilize these substrates. Based on sequence comparisons, carbonic anhydrases belong to three genetically distinct classes (␣, ␤, and ␥) which appear to have independent origins (24). The most extensively studied enzymes are those from the ␣-class, which is composed primarily of mammalian carbonic anhydrases, but also includes enzymes from the green alga Chlamydomonas reinhardtii (19,20) and the prokaryote Neisseria gonorrhoeae (13). The ␤-class enzymes are abundant in C 3 and C 4 monocotyledenous and dicotyledenous plants and green unicellular algae (24, 43), where they are essential for photosynthetic CO 2 fixation (6). The most recently identified class of carbonic anhydrase, the ␥-class (24), is represented by the prototype Cam from the archaeon Methanosarcina thermophila (2). Even though sequences encoding putative ␥-class carbonic anhydrases have been found in prokaryotes from both the Bacteria and Archaea domains (2...

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“…Recombinant CAIV contains 264 residues, with 57% sequence identity to human CAIV and 33% sequence identity to human CAII (identities based on alignment of tertiary structures). The maximal value of kca,/K,,, for C02 hydration exhibited by murine CAIV is 3 X lo7 M" s-I, threefold less than the corresponding value for human CAII or human CAIV, kc,, FJ 1 .O X lo5 s" at pH 7-8, which is 10-fold less than that of human CAIV (Hurt et al, 1997). Because kea, reflects proton transfer from zinc-bound water to His-64 in the second step of catalysis (Silverman & Lindskog, 1988), the structure of murine CAIV and its comparison with human CAN reveals clues regarding the molecular basis of impaired proton transfer in murine CAN.…”

mentioning

confidence: 74%

“…The truncated form lacks the C-terminal glycosylphosphatidylinositol (GPI) anchor, but appears to have full activity (Hurt et al, 1997). Recombinant CAIV contains 264 residues, with 57% sequence identity to human CAIV and 33% sequence identity to human CAII (identities based on alignment of tertiary structures).…”

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confidence: 99%

Structures of murine carbonic anhydrase IV and human carbonic anhydrase II complexed with brinzolamide: Molecular basis of isozyme‐drug discrimination

et al. 1998

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Carbonic anhydrase IV (CAIV) is a membrane-associated enzyme anchored to plasma membrane surfaces by a phosphatidylinositol glycan linkage. We have determined the 2.8-A resolution crystal structure of a truncated, soluble form of recombinant murine CAIV. We have also determined the structure of its complex with a drug used for glaucoma therapy, the sulfonamide inhibitor brinzolamide (Azoptm). The overall structure of murine CAIV is generally similar to that of human CAW, however, some local structural differences are found in the active site resulting from amino acid sequence differences in the "130's segment" and the residue-63 loop (these may affect the nearby catalytic proton shuttle, His-64). Similar to human CAN, the C-terminus of murine CAIV is surrounded by a substantial electropositive surface potential that may stabilize the interaction with the phospholipid membrane. Binding interactions observed for brinzolamide rationalize the generally weaker affinity of inhibitors used in glaucoma therapy toward CAIV compared with CAII.

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Catalytic Properties of Murine Carbonic Anhydrase IV

Cited by 40 publications

References 39 publications

Characterization of the B12- and Iron-Sulfur-containing Reductive Dehalogenase fromDesulfitobacterium chlororespirans

Characterization of the B12- and Iron-Sulfur-containing Reductive Dehalogenase fromDesulfitobacterium chlororespirans

Structural and Kinetic Characterization of an Archaeal β-Class Carbonic Anhydrase

Structures of murine carbonic anhydrase IV and human carbonic anhydrase II complexed with brinzolamide: Molecular basis of isozyme‐drug discrimination

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