In silico characterization of selected orchids’ hmg-coa reductases / (Record no. 104264)

MARC details
000 -LEADER
fixed length control field 03385ntm a2200337 i 4500
003 - CONTROL NUMBER IDENTIFIER
control field MY-KuUP
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20260303131916.0
006 - FIXED-LENGTH DATA ELEMENTS--ADDITIONAL MATERIAL CHARACTERISTICS
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007 - PHYSICAL DESCRIPTION FIXED FIELD--GENERAL INFORMATION
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fixed length control field 260303t20252025my a|||fs|||| 000 0 eng d
020 ## - INTERNATIONAL STANDARD BOOK NUMBER
International Standard Book Number THE0010413 (Local)
Qualifying information Hardback
040 ## - CATALOGING SOURCE
Original cataloging agency UMPSA
Language of cataloging eng
Transcribing agency UMPSA
Description conventions rda
090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN)
Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) FIST .S939 2025 r Bc.
100 0# - MAIN ENTRY--PERSONAL NAME
Personal name Nurul Syazana Aqila Binti Muhammad Zawawi,
Relator term author.
245 10 - TITLE STATEMENT
Title In silico characterization of selected orchids’ hmg-coa reductases /
Statement of responsibility, etc. Nurul Syazana Aqila Binti Muhammad Zawawi
264 #1 - PRODUCTION, PUBLICATION, DISTRIBUTION, MANUFACTURE, AND COPYRIGHT NOTICE
Place of production, publication, distribution, manufacture Kuantan, Pahang :
Name of producer, publisher, distributor, manufacturer UMPSA,
Date of production, publication, distribution, manufacture, or copyright notice 2025
264 #4 - PRODUCTION, PUBLICATION, DISTRIBUTION, MANUFACTURE, AND COPYRIGHT NOTICE
Date of production, publication, distribution, manufacture, or copyright notice © 2025
300 ## - PHYSICAL DESCRIPTION
Extent xiii, 116 pages :
Other physical details illustrations ;
336 ## - CONTENT TYPE
Source rdacontent
Content type term text
337 ## - MEDIA TYPE
Source rdamedia
Media type term unmediated
338 ## - CARRIER TYPE
Source rdacarrier
Carrier type term volume
347 ## - DIGITAL FILE CHARACTERISTICS
Source rda
File type text file
Encoding format PDF
500 ## - GENERAL NOTE
General note Faculty of Industrial Sciences and Technology
502 ## - DISSERTATION NOTE
Dissertation note Final Year Report (Bachelor of Applied Science in Industrial Biotechnology) -- Universiti Malaysia Pahang Al-Sultan Abdullah - 2025
504 ## - BIBLIOGRAPHY, ETC. NOTE
Bibliography, etc. note HMG-CoA reductase (HMGR) was an essential enzyme for producing mevalonate, a key component of floral scent in orchids. It acted as a catalyst in the mevalonate pathway. This process yielded various isoprenoid compounds, including those contributing to the floral aroma. This study investigated the structure and function of HMGR and its homologous proteins in five orchid species which were Vanda Mimi Palmer, Phalaenopsis equestris, Dendrobium nobile, Dendrobium catenatum, and Vanilla planifolia, using an in silico approach.Amino acid sequences available in the NCBI GenBank were utilized to perform homology modeling and predict the threedimensional (3D) structures of HMGR and its related proteins. The reliability of these structural models was validated using VERIFY 3D, PROCHECK, and ERRAT tools. The study aimed to predict the 3D-protein structure of the selected orchids' HMG-CoA reductases and homologous proteins using a homology modeling approach and to investigate the binding positions of potential ligands to the 3D structure of these enzymes by molecular docking. Active pocket regions (R1 and R2) were identified using CASTp, where R1 was the predicted pocket binding site of the selected orchid HMGRs and homologous proteins, while R2 was the predicted pocket binding site for 8ECG. Molecular docking experiments were conducted to evaluate the binding sites and affinities of potential substrates (HMG-CoA, Acetyl-CoA, and Acetoacetyl-CoA) and their product, mevalonate. Protein-ligand docking studies were performed using Autodock Vina to predict the orientation of a ligand bound to the protein and compare it with the predicted active site pocket analysis. This study contributed to a deeper understanding of the molecular and functional properties of HMGR and its homologous proteins in orchids. These insights enhanced knowledge of floral scent biosynthesis, particularly the enzymatic pathways involving HMG-CoA reductases, and provided valuable information for potential applications in horticulture, the fragrance industry, and related fields
610 20 - SUBJECT ADDED ENTRY--CORPORATE NAME
Corporate name or jurisdiction name as entry element Faculty of Industrial Sciences and Technology
General subdivision Dissertations
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element Universities and colleges
General subdivision Dissertations
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element Final Year Report
General subdivision Dissertations
856 ## - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier http://umpir.ump.edu.my/id/eprint/45761
942 ## - ADDED ENTRY ELEMENTS (KOHA)
Source of classification or shelving scheme Library of Congress Classification
Koha item type Thesis
Holdings
Withdrawn status Lost status Source of classification or shelving scheme Damaged status Not for loan Permanent Location Current Location Date acquired Total Checkouts Full call number Barcode Date last seen Price effective from Koha item type
  Not lost Library of Congress Classification     UMPLIB GAMBANG UMPLIB GAMBANG 03/03/2026   FIST .S939 2025 r Bc. T000003731 03/03/2026 03/03/2026 Final Year Report

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