Functional analysis of conserved histidine residues in Cephalosporium acremonium isopenicillin N synthase by site-directed mutagenesis.

about

Cloning and expression analysis of the pcbAB-pcbC beta-lactam genes in the marine fungus Kallichroma tethys.Identification of strictly conserved histidine and arginine residues as part of the active site in Petunia hybrida flavanone 3beta-hydroxylase.

P2860

Q31130645-0C0D5FCF-C89A-4CAA-A5C8-69ADB3FFCE0B Q38341544-5255AD8D-36E7-4BAB-AA12-1CBD42A4D817

P2860

Functional analysis of conserved histidine residues in Cephalosporium acremonium isopenicillin N synthase by site-directed mutagenesis.

Item

http://www.wikidata.org/entity/Q54595296

description

1996 nî lūn-bûn

@nan

1996年の論文

@ja

1996年学术文章

@wuu

1996年学术文章

@zh-cn

1996年学术文章

@zh-hans

1996年学术文章

@zh-my

1996年学术文章

@zh-sg

1996年學術文章

@yue

1996年學術文章

@zh

1996年學術文章

@zh-hant

name

Functional analysis of conserv ...... by site-directed mutagenesis.

@en

Functional analysis of conserv ...... by site-directed mutagenesis.

@nl

type

Item

label

Functional analysis of conserv ...... by site-directed mutagenesis.

@en

Functional analysis of conserv ...... by site-directed mutagenesis.

@nl

prefLabel

Functional analysis of conserv ...... by site-directed mutagenesis.

@en

Functional analysis of conserv ...... by site-directed mutagenesis.

@nl

P1476

Functional analysis of conserv ...... by site-directed mutagenesis.

@en

P2093

Sim TS

http://www.w3.org/2001/XMLSchema#string

Tan DS

http://www.w3.org/2001/XMLSchema#string

P2860

DNA sequencing with chain-terminating inhibitors

Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes

Rapid and efficient site-specific mutagenesis without phenotypic selection

NMR studies of the active site of isopenicillin N synthase, a non-heme iron(II) enzyme.

Cloning and characterization of the isopenicillin N synthase gene of Streptomyces griseus NRRL 3851 and studies of expression and complementation of the cephamycin pathway in Streptomyces clavuligerus

Analysis of the role of cysteine residues in isopenicillin N synthetase activity by site-directed mutagenesis.

Penicillin and cephalosporin biosynthetic genes: structure, organization, regulation, and evolution.

P304

889-894

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.271.2.889

http://www.w3.org/2001/XMLSchema#string

P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

271

http://www.w3.org/2001/XMLSchema#string

P577

1996-01-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

14642227

http://www.w3.org/2001/XMLSchema#string

P698

8557701

http://www.w3.org/2001/XMLSchema#string

Functional analysis of conserved histidine residues in Cephalosporium acremonium isopenicillin N synthase by site-directed mutagenesis.

about

P2860

P2860

Functional analysis of conserved histidine residues in Cephalosporium acremonium isopenicillin N synthase by site-directed mutagenesis.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698