Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxyogenase

被引：20

作者：

Brown, CK ^{[1
]}

Vetting, MW

Earhart, CA

Ohlendorf, DH

机构：

[1] Ctr Met Biocatalysis, Minneapolis, MN 55455 USA

[2] Dept Biochem Mol Biol & Biophys, Minneapolis, MN 55455 USA

[3] Albert Einstein Coll Med, Dept Biochem, Bronx, NY 10461 USA

来源：

ANNUAL REVIEW OF MICROBIOLOGY | 2004年 / 58卷

关键词：

catechol; protocatechuate; dioxygenase; metalloenzyme; iron; crystallography;

D O I：

10.1146/annurev.micro.57.030502.090927

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The catechol dioxygenases allow a wide variety of bacteria to use aromatic compounds as carbon sources by catalyzing the key ring-opening step. These enzymes use specifically either catechol or protocatechuate (2,3-dihydroxybenozate) as their substrates; they use a bare metal ion as the sole cofactor. To learn how this family of metalloenzymes functions, a structural analysis of designed and selected mutants of these enzymes has been undertaken. Here we review the results of this analysis on the nonheme ferric iron intradiol dioxygenase protocatechuate 3,4-dioxygenase.

引用

收藏

页码：555 / 585

页数：39

相关论文

共 117 条

[21] Spectroscopic and electronic structure studies of protocatechuate 3,4-dioxygenase: Nature of tyrosinate-Fe(III) bonds and their contribution to reactivity [J].

Davis, MI ;

Orville, AM ;

Neese, F ;

Zaleski, JM ;

Lipscomb, JD ;

Solomon, EI .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2002, 124 (04) :602-614

[22]

Delano WL., 2002, The PyMOL Molecular Graphics System

[23] Evolution of functional diversity in the cupin superfamily [J].

Dunwell, JM ;

Culham, A ;

Carter, CE ;

Sosa-Aguirre, CR ;

Goodenough, PW .

TRENDS IN BIOCHEMICAL SCIENCES, 2001, 26 (12) :740-746

[24] Microbial relatives of the seed storage proteins of higher plants: Conservation of structure and diversification of function during evolution of the cupin superfamily [J].

Dunwell, JM ;

Khuri, S ;

Gane, PJ .

MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS, 2000, 64 (01) :153-+

[25]

DURHAM DR, 1980, BIOCHEMISTRY-US, V19, P149, DOI 10.1021/bi00542a023

[26] PRELIMINARY CRYSTALLOGRAPHIC STUDY OF PROTOCATECHUATE 3,4-DIOXYGENASE FROM BREVIBACTERIUM-FUSCUM [J].

EARHART, CA ;

RADHAKRISHNAN, R ;

ORVILLE, AM ;

LIPSCOMB, JD ;

OHLENDORF, DH .

JOURNAL OF MOLECULAR BIOLOGY, 1994, 236 (01) :374-376

[27] Crystal structure and resonance Raman studies of protocatechuate 3,4-dioxygenase complexed with 3,4-dihydroxyphenylacetate [J].

Elgren, TE ;

Orville, AM ;

Kelly, KA ;

Lipscomb, JD ;

Ohlendorf, DH ;

Que, L .

BIOCHEMISTRY, 1997, 36 (38) :11504-11513

[28] Characterization of a protocatechuate catabolic gene cluster from Rhodococcus opacus 1CP:: Evidence for a merged enzyme with 4-carboxymuconolactone-decarboxylating and 3-oxoadipate enol-lactone-hydrolyzing activity [J].

Eulberg, D ;

Lakner, S ;

Golovleva, LA ;

Schlömann, M .

JOURNAL OF BACTERIOLOGY, 1998, 180 (05) :1072-1081

[29] BIODEGRADATION OF XENOBIOTIC AND OTHER PERSISTENT COMPOUNDS - THE CAUSES OF RECALCITRANCE [J].

FEWSON, CA .

TRENDS IN BIOTECHNOLOGY, 1988, 6 (07) :148-153

[30] The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing endosymbiont Sinorhizobium meliloti [J].

Finan, TM ;

Weidner, S ;

Wong, K ;

Buhrmester, J ;

Chain, P ;

Vorhölter, FJ ;

Hernandez-Lucas, I ;

Becker, A ;

Cowie, A ;

Gouzy, J ;

Golding, B ;

Pühler, A .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (17) :9889-9894

← 1 2 3 4 5 6 7 8 9 10 →